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Sample records for albumin bsa nanoparticles

  1. Gold nanoparticles: BSA (Bovine Serum Albumin) coating and X-ray irradiation produce variable-spectrum photoluminescence

    International Nuclear Information System (INIS)

    We show that by using different x-ray irradiation times of BSA-coated Au nanoparticles (NPs) we can change their ultraviolet-stimulated photoluminescence and shift the spectral weight over the visible spectral range. This is due to the interplay of two emission bands, one due to BSA and the other related to gold. The emission properties did not change with time over a period of several months. - Highlights: • Gold nanoparticles (Au NPs) coated with Bovine Serum Albumin (BSA) are synthesized by x-ray irradiation. • BSA coated AuNPs with ∼1 nm size show strong photoluminescence in red by UV excitation. • The blue photoluminescence of BSA increase with x-ray irradiation. • Increase x-ray irradiation time during the synthesis shift the color of the colloid from red to blue

  2. Gold nanoparticles: BSA (Bovine Serum Albumin) coating and X-ray irradiation produce variable-spectrum photoluminescence

    Energy Technology Data Exchange (ETDEWEB)

    Lee, Kuo-Hao [Department of Electrophysics, National Chiao Tung University, Hsinchu, Taiwan (China); Institute of Physics, Academia Sinica, Taipei 115, Taiwan (China); Lai, Sheng-Feng [Institute of Physics, Academia Sinica, Taipei 115, Taiwan (China); Department of Engineering Science, National Cheng Kung University, Tainan 701, Taiwan (China); Lin, Yan-Cheng; Chou, Wu-Ching [Department of Electrophysics, National Chiao Tung University, Hsinchu, Taiwan (China); Ong, Edwin B.L. [Institute of Physics, Academia Sinica, Taipei 115, Taiwan (China); Tan, Hui-Ru [Institute of Materials Research and Engineering, 3 Research Link, 117602 (Singapore); Tok, Eng Soon [Physics Department, National University of Singapore, 117542 (Singapore); Yang, C.S. [Center for Nanomedicine, National Health Research Institutes, Miaoli 350, Taiwan (China); Margaritondo, G. [Ecole Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne (Switzerland); Hwu, Y., E-mail: phhwu@sinica.edu.tw [Institute of Physics, Academia Sinica, Taipei 115, Taiwan (China); Advanced Optoelectronic Technology Center, National Cheng Kung University, Tainan 701, Taiwan (China); Institute of Optoelectronic Sciences, National Taiwan Ocean University, Keelung 202, Taiwan (China)

    2015-01-15

    We show that by using different x-ray irradiation times of BSA-coated Au nanoparticles (NPs) we can change their ultraviolet-stimulated photoluminescence and shift the spectral weight over the visible spectral range. This is due to the interplay of two emission bands, one due to BSA and the other related to gold. The emission properties did not change with time over a period of several months. - Highlights: • Gold nanoparticles (Au NPs) coated with Bovine Serum Albumin (BSA) are synthesized by x-ray irradiation. • BSA coated AuNPs with ∼1 nm size show strong photoluminescence in red by UV excitation. • The blue photoluminescence of BSA increase with x-ray irradiation. • Increase x-ray irradiation time during the synthesis shift the color of the colloid from red to blue.

  3. Conjugation of nano and quantum materials with bovine serum albumin (BSA) to study their biological potential

    International Nuclear Information System (INIS)

    Conjugates of gold nanoparticles (AuNPs) and semiconductor quantum dots (CdS/T) have been synthesized with bovine serum albumin (BSA) using wet chemistry. The optical properties of nano and quantum materials and their BSA conjugate have been studied using UV–Visible and Fluorescence spectroscopy. UV–Visible spectrum of pure BSA showed an absorption maximum at 278 nm, which showed blue shift after its conjugation with nano and quantum materials. Increased concentration of AuNPs during conjugation resulted in broadening of BSA peak (278 nm), which can be related to the formation of ground state complex formation, caused by the partial adsorption of BSA on the surface of NPs. However, increased concentrations of BSA resulted in decrease in SPR intensity of gold nanoparticles (528 nm) and absorbance peak of BSA started diminishing. AuNPs acted as quencher for BSA fluorescence intensity, when excited at 280 nm. The binding constant (K) and the number of binding sites (n) between AuNPs and BSA have been found to be 1.97×102 LM−1 and 0.6 respectively. With quantum dots, conjugation resulted in enhancement of fluorescence emission of quantum dots when excited at 300 nm, which might be due to the stabilizing effect of BSA on QDs or due to energy transfer from tryptophan moieties of albumin to quantum dots. -- Highlights: • Synthesis of nanoparticles (AuNPs) and quantum dots (CdS). • Conjugation of these materials with bovine serum albumin. • Optical behavioral studies

  4. Conjugation of nano and quantum materials with bovine serum albumin (BSA) to study their biological potential

    Energy Technology Data Exchange (ETDEWEB)

    Singh, Suman, E-mail: sumansingh01@gmail.com [Central Scientific Instruments Organisation (CSIR-CSIO), Chandigarh (India); Kaur, Rajnish; Chahal, Jitender; Devi, P. [Central Scientific Instruments Organisation (CSIR-CSIO), Chandigarh (India); Jain, D.V.S. [Panjab University, Chandigarh (India); Singla, M.L., E-mail: singla_min@yahoo.co.in [Central Scientific Instruments Organisation (CSIR-CSIO), Chandigarh (India)

    2013-09-15

    Conjugates of gold nanoparticles (AuNPs) and semiconductor quantum dots (CdS/T) have been synthesized with bovine serum albumin (BSA) using wet chemistry. The optical properties of nano and quantum materials and their BSA conjugate have been studied using UV–Visible and Fluorescence spectroscopy. UV–Visible spectrum of pure BSA showed an absorption maximum at 278 nm, which showed blue shift after its conjugation with nano and quantum materials. Increased concentration of AuNPs during conjugation resulted in broadening of BSA peak (278 nm), which can be related to the formation of ground state complex formation, caused by the partial adsorption of BSA on the surface of NPs. However, increased concentrations of BSA resulted in decrease in SPR intensity of gold nanoparticles (528 nm) and absorbance peak of BSA started diminishing. AuNPs acted as quencher for BSA fluorescence intensity, when excited at 280 nm. The binding constant (K) and the number of binding sites (n) between AuNPs and BSA have been found to be 1.97×10{sup 2} LM{sup −1} and 0.6 respectively. With quantum dots, conjugation resulted in enhancement of fluorescence emission of quantum dots when excited at 300 nm, which might be due to the stabilizing effect of BSA on QDs or due to energy transfer from tryptophan moieties of albumin to quantum dots. -- Highlights: • Synthesis of nanoparticles (AuNPs) and quantum dots (CdS). • Conjugation of these materials with bovine serum albumin. • Optical behavioral studies.

  5. On the mechanical properties of bovine serum albumin (BSA) adhesives.

    Science.gov (United States)

    Berchane, N S; Andrews, M J; Kerr, S; Slater, N K H; Jebrail, F F

    2008-04-01

    Biological adhesives, natural and synthetic, are of current active interest. These adhesives offer significant advantages over traditional sealant techniques, in particular, they are easier to use, and can play an integral part in the healing mechanism of tissue. Thus, biological adhesives can play a major role in medical applications if they possess adequate mechanical behavior and stability over time. In this work, we report on the method of preparation of bovine serum albumin (BSA) into a biological adhesive. We present quantitative measurements that show the effect of BSA concentration and cross-linker content on the bonding strength of BSA adhesive to wood. A comparison is then made with synthetic poly(glycidyl methacrylate) (PGMA) adhesive, and a commercial cyanoacrylate glue, which was used as a control adhesive. In addition, BSA samples were prepared and characterized for their water content, tensile strength, and elasticity. We show that on dry surface, BSA adhesive exhibits a high bonding strength that is comparable with non-biological commercial cyanoacrylate glues, and synthetic PGMA adhesive. Tensile testing on wet wood showed a slight increase in the bonding strength of BSA adhesive, a considerable decrease in the bonding strength of cyanoacrylate glue, and negligible adhesion of PGMA. Tests performed on BSA samples demonstrate that initial BSA concentration and final water content have a significant effect on the stress-strain behavior of the samples. PMID:18197367

  6. Synthesis and Characterization of BSA Conjugated Silver Nanoparticles (Ag/BSA Nanoparticles) and Evaluation of Biological Properties of Ag/BSA Nanoparticles and Ag/BSA Nanoparticles Loaded Poly(hydroxy butyrate valerate) PHBV Films

    Science.gov (United States)

    Ambaye, Almaz

    Staphylococcus aureus, Escherichia coli and Pseudomonas aeruginosa are the etiological agents of several infectious diseases. Antibiotic resistance by these three microbes has emerged as a prevalent problem due in part to the misuse of existing antibiotics and the lack of novel antibiotics. Nanoparticles have emerged as an alternative antibacterial agents to conventional antibiotics owing to their high surface area to volume ratio and their unique chemical and physical properties. Among the nanoparticles, silver nanoparticles have gained increasing attention because silver nanoparticles exhibit antibacterial activity against a range of gram positive and gram negative bacteria. Nanoparticles of well-defined chemistry and morphology can be used in broad biomedical applications, especially in bone tissue engineering applications, where bone infection by bacteria can be acute and lethal. It is commonly noted in the literature that the activity of nanoparticles against microorganisms is dependent upon the size and concentration of the nanoparticles as well as the chemistry of stabilizing agent. To the best of our knowledge, a comprehensive study that evaluates the antibacterial activity of well characterized silver nanoparticles in particular Bovine Serum Albumin (BSA) stabilized against S. aureus and E. coli and cytotoxicity level of BSA stabilized silver nanoparticles towards osteoblast cells (MC3T3-E1) is currently lacking. Therefore, the primary objective of this study was to characterize protein conjugated silver nanoparticles prepared by chemical reduction of AgNO3 and BSA mixture. The formation of Ag/BSA nanoparticles was studied by UV-Vis spectroscopy. The molar ratio of silver to BSA in the Ag/BSA nanoparticles was established to be 27+/- 3: 1, based on Thermogravimetric Analysis and Atomic Absorption Spectroscopy. Based on atomic force microscopy, dynamic light scattering,and transmission electron microscopy(TEM) measurements, the particle size (diameter) of

  7. SANS study of interaction of silica nanoparticles with BSA protein and their resultant structure

    Science.gov (United States)

    Yadav, Indresh; Aswal, V. K.; Kohlbrecher, J.

    2014-04-01

    Small angle neutron scattering (SANS) has been carried out to study the interaction of anionic silica nanoparticles (88 Å) with globular protein Bovine Serum Albumin (BSA) (M.W. 66.4 kD) in aqueous solution. The measurements have been carried out on fixed concentration (1 wt %) of Ludox silica nanoparticles with varying concentration of BSA (0-5 wt %) at pH7. Results show that silica nanoparticles and BSA coexist as individual entities at low concentration of BSA where electrostatic repulsive interactions between them prevent their aggregation. However, as the concentration of BSA increases (≥ 0.5 wt %), it induces the attractive depletion interaction among nanoparticles leading to finally their aggregation at higher BSA concentration (2 wt %). The aggregates are found to be governed by the diffusion limited aggregation (DLA) morphology of fractal nature having fractal dimension about 2.4.

  8. SANS study of interaction of silica nanoparticles with BSA protein and their resultant structure

    Energy Technology Data Exchange (ETDEWEB)

    Yadav, Indresh, E-mail: vkaswal@barc.gov.in; Aswal, V. K., E-mail: vkaswal@barc.gov.in [Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai-400085 (India); Kohlbrecher, J. [Laboratory for Neutron Scattering, Paul Scherrer Institute, CH-5232 PSI Villigen Switzerland (Switzerland)

    2014-04-24

    Small angle neutron scattering (SANS) has been carried out to study the interaction of anionic silica nanoparticles (88 Å) with globular protein Bovine Serum Albumin (BSA) (M.W. 66.4 kD) in aqueous solution. The measurements have been carried out on fixed concentration (1 wt %) of Ludox silica nanoparticles with varying concentration of BSA (0–5 wt %) at pH7. Results show that silica nanoparticles and BSA coexist as individual entities at low concentration of BSA where electrostatic repulsive interactions between them prevent their aggregation. However, as the concentration of BSA increases (≥ 0.5 wt %), it induces the attractive depletion interaction among nanoparticles leading to finally their aggregation at higher BSA concentration (2 wt %). The aggregates are found to be governed by the diffusion limited aggregation (DLA) morphology of fractal nature having fractal dimension about 2.4.

  9. SYNTHESIS AND CHARACTERIZATION OF SURFACE-HYPERBRANCHED MAGNETITE NANOPARTICLE FOR BOVINE SERUM ALBUMIN IMMOBILIZATION

    Institute of Scientific and Technical Information of China (English)

    Bifeng Pan; Feng Gao; Hongchen Gu

    2004-01-01

    A hyperbranched polyamidoamine polymer was synthesized on the surface of magnetite nanoparticles to enhance bovine serum albumin (BSA) immobilization efficiency. The amount of immobilized bovine serum albumin (BSA)on the surface-hyperbranched magnetite nanoparticle was up to 2.5 times as much as that of magnetite nanoparticle modified with only amino silane.

  10. Production of BSA-poly(ethyl cyanoacrylate) nanoparticles as a coating material that improves wetting property

    Science.gov (United States)

    Alkyl cyanoacrylates have long been used for the synthesis of colloidal nanoparticles. In the involved polymerization reaction, OH- ions derived from dissociation of water have been used as an initiator. In the current research, an animal protein, bovine serum albumin (BSA) molecules were utilized a...

  11. In situ synthesized BSA capped gold nanoparticles: Effective carrier of anticancer drug Methotrexate to MCF-7 breast cancer cells

    Energy Technology Data Exchange (ETDEWEB)

    Murawala, Priyanka [Physical and Materials Chemistry Division, National Chemical Laboratory, Pune 411008 (India); Tirmale, Amruta [Physical and Materials Chemistry Division, National Chemical Laboratory, Pune 411008 (India); National Centre for Cell Science, NCCS, Pune 411007 (India); Shiras, Anjali, E-mail: anjalishiras@nccs.res.in [National Centre for Cell Science, NCCS, Pune 411007 (India); Prasad, B.L.V., E-mail: pl.bhagavatula@ncl.res.in [Physical and Materials Chemistry Division, National Chemical Laboratory, Pune 411008 (India)

    2014-01-01

    The proficiency of MTX loaded BSA capped gold nanoparticles (Au-BSA-MTX) in inhibiting the proliferation of breast cancer cells MCF-7 as compared to the free drug Methotrexate (MTX) is demonstrated based on MTT and Ki-67 proliferation assays. In addition, DNA ladder gel electrophoresis studies, flow cytometry and TUNEL assay confirmed the induction of apoptosis by MTX and Au-BSA-MTX in MCF-7 cells. Notably, Au-BSA-MTX was found to have higher cytotoxicity on MCF-7 cells compared with an equivalent dose of free MTX. The enhanced activity is attributed to the preferential uptake of Au-BSA-MTX particles by MCF-7 cells due to the presence of BSA that acts as a source of nutrient and energy to the rapidly proliferating MCF-7 cells. Moreover, the targeting ability of the drug MTX to the over expressed folate receptors on MCF-7 cells also contributes to the enhanced uptake and activity. Taken together, these results unveil that Au-BSA-MTX could be more effective than free drug for cancer treatment. - Highlights: • Gold nanoparticles prepared using bovine serum albumin as a reducing and capping agent. • These gold nanoparticles are extremely stable under strong electrolyte and pH conditions. • The anticancer drug methotrexate has been loaded on the Au-BSA nanoparticles. • Due to BSA loading these are taken up by cancerous cells preferentially. • Better proficiency in inhibiting MCF-7 cells as compared to the free drug Methotrexate is demonstrated.

  12. In situ synthesized BSA capped gold nanoparticles: Effective carrier of anticancer drug Methotrexate to MCF-7 breast cancer cells

    International Nuclear Information System (INIS)

    The proficiency of MTX loaded BSA capped gold nanoparticles (Au-BSA-MTX) in inhibiting the proliferation of breast cancer cells MCF-7 as compared to the free drug Methotrexate (MTX) is demonstrated based on MTT and Ki-67 proliferation assays. In addition, DNA ladder gel electrophoresis studies, flow cytometry and TUNEL assay confirmed the induction of apoptosis by MTX and Au-BSA-MTX in MCF-7 cells. Notably, Au-BSA-MTX was found to have higher cytotoxicity on MCF-7 cells compared with an equivalent dose of free MTX. The enhanced activity is attributed to the preferential uptake of Au-BSA-MTX particles by MCF-7 cells due to the presence of BSA that acts as a source of nutrient and energy to the rapidly proliferating MCF-7 cells. Moreover, the targeting ability of the drug MTX to the over expressed folate receptors on MCF-7 cells also contributes to the enhanced uptake and activity. Taken together, these results unveil that Au-BSA-MTX could be more effective than free drug for cancer treatment. - Highlights: • Gold nanoparticles prepared using bovine serum albumin as a reducing and capping agent. • These gold nanoparticles are extremely stable under strong electrolyte and pH conditions. • The anticancer drug methotrexate has been loaded on the Au-BSA nanoparticles. • Due to BSA loading these are taken up by cancerous cells preferentially. • Better proficiency in inhibiting MCF-7 cells as compared to the free drug Methotrexate is demonstrated

  13. Suppressing the cytotoxicity of CuO nanoparticles by uptake of curcumin/BSA particles

    Science.gov (United States)

    Zhang, Wenjing; Jiang, Pengfei; Chen, Ying; Luo, Peihua; Li, Guanqun; Zheng, Botuo; Chen, Wei; Mao, Zhengwei; Gao, Changyou

    2016-05-01

    The adverse effects of metal-based nanoparticles on human beings and the environment have received extensive attention recently. It is urgently required to develop a simple and effective method to suppress the toxicity of metal-based nanomaterials. In this study, a hydrophobic antioxidant and a chelation agent curcumin (CUR) were encapsulated into bovine serum albumin (BSA) particles by a simple co-precipitation method, and followed by glutaraldehyde cross-linking. The CUR/BSA particles had an average size of 300 nm in diameter with a negatively charged surface and sustained curcumin release properties. The cellular uptake and cytotoxicity of CUR/BSA particles were followed on A549 cells, HepG2 cells and RAW264.7 cells. The CUR/BSA particles had higher intracellular accumulation and lower cytotoxicity compared with the free curcumin at the same drug concentration. The CUR/BSA particles could suppress the cytotoxicity generated by CuO nanoparticles as a result of decrease of both the intracellular reactive oxygen species (ROS) level and Cu2+ concentration, while the free curcumin did not show any obvious detoxicating effect. The detoxicating effects of CUR/BSA particles were further studied in an intratracheal instillation model in vivo, demonstrating significant reduction of toxicity and inflammatory response in rat lungs induced by CuO nanoparticles. The concept-proving study demonstrates the potential of the CUR/BSA particles in suppressing cytotoxicity of metal-based nanomaterials, which is a paramount requirement for the safe application of nanotechnology.

  14. Suppressing the cytotoxicity of CuO nanoparticles by uptake of curcumin/BSA particles.

    Science.gov (United States)

    Zhang, Wenjing; Jiang, Pengfei; Chen, Ying; Luo, Peihua; Li, Guanqun; Zheng, Botuo; Chen, Wei; Mao, Zhengwei; Gao, Changyou

    2016-05-01

    The adverse effects of metal-based nanoparticles on human beings and the environment have received extensive attention recently. It is urgently required to develop a simple and effective method to suppress the toxicity of metal-based nanomaterials. In this study, a hydrophobic antioxidant and a chelation agent curcumin (CUR) were encapsulated into bovine serum albumin (BSA) particles by a simple co-precipitation method, and followed by glutaraldehyde cross-linking. The CUR/BSA particles had an average size of 300 nm in diameter with a negatively charged surface and sustained curcumin release properties. The cellular uptake and cytotoxicity of CUR/BSA particles were followed on A549 cells, HepG2 cells and RAW264.7 cells. The CUR/BSA particles had higher intracellular accumulation and lower cytotoxicity compared with the free curcumin at the same drug concentration. The CUR/BSA particles could suppress the cytotoxicity generated by CuO nanoparticles as a result of decrease of both the intracellular reactive oxygen species (ROS) level and Cu(2+) concentration, while the free curcumin did not show any obvious detoxicating effect. The detoxicating effects of CUR/BSA particles were further studied in an intratracheal instillation model in vivo, demonstrating significant reduction of toxicity and inflammatory response in rat lungs induced by CuO nanoparticles. The concept-proving study demonstrates the potential of the CUR/BSA particles in suppressing cytotoxicity of metal-based nanomaterials, which is a paramount requirement for the safe application of nanotechnology. PMID:27098928

  15. Interaction and sonodynamic damage activity of acridine red (AD-R) to bovine serum albumin (BSA)

    Energy Technology Data Exchange (ETDEWEB)

    Chen, Dandan; Xie, Jinhui; Wu, Qiong; Fan, Ping; Wang, Jun, E-mail: wangjun888tg@126.com

    2015-04-15

    The sonodynamic therapy (SDT) has become an attractive antitumor treatment method in recent years, but the selection of sonosensitizer, mechanism of damage biomolecule and kind of reactive oxygen species (ROS) generated during sonodynamic process have not been investigated in detail. In this paper, the acridine red (AD-R), as a sonosensitizer, combining with ultrasonic irradiation to damage bovine serum albumin (BSA) was investigated. At first, the interaction of AD-R to BSA molecules in aqueous solution was studied by fluorescence spectroscopy. As judged from the experimental results, the quenching mechanism of BSA fluorescence belongs to a static process. Synchronous fluorescence spectra demonstrate that the binding and damage sites to BSA molecules are mainly on the tryptophan residues. The generation and kind of generated ROS were also estimated by the method of oxidation and extraction photometry. This paper may offer some valuable references for the study of the sonodynamic activity and application of AD-R in SDT for tumor treatment. - Highlights: ●Acridine red (AD-R) is used to study interaction with BSA. ●Spectroscopy is used to study sonodynamic damage activity of AD-R to BSA. ●Generation of ROS caused by AD-R under ultrasonic irradiation was determined.

  16. Uptake of albumin nanoparticle surface modified with glycyrrhizin by primary cultured rat hepatocytes

    Institute of Scientific and Technical Information of China (English)

    Sheng-Jun Mao; Shi-Xiang Hou; Ru He; Liang-Ke Zhang; Da-Peng Wei; Yue-Qi Bi; Hui Jin

    2005-01-01

    AIM: To investigate the uptake difference between bovine serum albumin nanoparticle (BSA-NP) and bovine serum albumin nanoparticles with their surface modified byglycyrrhizin (BSA-NP-GL) and to develop a novel hepatocyte targeting BSA-NP-GL based on active targeting technology mediated by specific binding site of GL on rat cellular membrane. METHODS: Calcein loaded bovine serum albumin nanoparticles (Cal-BSA-NP) were prepared by desolvation process. Glycyrrhizin was conjugated to the surface reactive amino groups (SRAG) of Cal-BSA-NP by sodium periodate oxidization, which resulted in calcein-loaded bovine serum albumin nanoparticles with their surface modified by glycyrrhizin (Cal-BSA-NP-GL). The morphology of the two types of prepared nanoparticles (NP) was observed by transmission electron microscopy. The diameter of NP was measured with a laser particle size analyzer. The interaction between Cal-BSA-NP-GL and primary cultured hepatocytes was studied through cellular uptake experiments. The uptake amount of Cal-BSA-NPGL and Cal-BSA-NP by rat hepatocytes was determinedby fluorospectrophotometry. Uptake characteristics were investigated through experiments of competitive inhibition of specific binding site of GL. RESULTS: Both Cal-BSA-NP-GL and Cal-BSA-NP had regular spherical surfaces. The average diameter of CalBSA-NP-GL and Cal-BSA-NP was 77 and 79 nm respectively. The uptake amount of the two NP by hepatocytes reached its maximum at 2 h after incubation. The uptake amount of Cal-BSA-NP-GL by rat hepatocytes was 4.43-fold higher than that of Cal-BSA-NP. There was a significant difference in the uptake of Cal-BSA-NP-GL and Cal-BSA-NP by hepatocytes (P<0.01). The uptake of Cal-BSA-NP-GL was inhibited when GL was added previously to isolated rat hepatocytes, and the uptake of Cal-BSA-NP was not affected by GL.CONCLUSION: A binding site of GL is present on the surface of rat hepatocytes, BSA-NP-GL may be internalized via this site by hepatocytes and can be used as

  17. Spectrometry researches on interaction and sonodynamic damage of riboflavin (RF) to bovine serum albumin (BSA)

    Science.gov (United States)

    Wang, Zhiqiu; Li, Jushi; Wang, Jun; Zou, Mingming; Wang, Siyu; Li, Ying; Kong, Yumei; Xia, Lixin

    2012-02-01

    In this paper, the riboflavin (RF) was used to study the interaction and sonodynamic damage to bovine serum albumin (BSA) by fluorescence and UV-vis spectroscopy. The results showed that the RF could efficiently bind to BSA in aqueous solution. Under ultrasonic irradiation, the RF could obviously damage the BSA. In addition, synchronous fluorescence spectroscopy revealed that the RF showed more accessible to tryptophan (Trp) residues than to tyrosine (Tyr) residues. Also, it damaged Trp residues more seriously than Tyr residues under ultrasonic irradiation. At last, the generation of reactive oxygen species (ROS) in sonodynamic process was estimated by the method of Oxidation-Extraction Spectrometry (OES). And then, several radical scavengers were used to determine the kind of ROS. It was found that at least the singlet oxygen ( 1O 2) and hydroxyl radicals ( rad OH) were generated.

  18. Size-controllable preparation of bovine serum albumin-conjugated PbS nanoparticles

    International Nuclear Information System (INIS)

    Protein-conjugated PbS nanocrystals with the average sizes of 15, 25, and 35 nm have been synthesized by adjusting the concentration of the bovine serum albumin (BSA) solution at room temperature. The obtained BSA-conjugated PbS nanoparticles have been characterized by powder X-ray diffraction, transmission electron microscopy, selected-area electron diffraction, high-resolution transmission electron microscopy, thermal analyses and photoluminescence. The quantum-confined effect of the BSA-conjugated PbS nanoparticles has been confirmed by the UV-vis spectra. The results indicated that the BSA not only induced the nucleation, but inhibited the further growth of PbS nanocrystals. The effect of Pb2+ on BSA and the change of BSA conformation were studied through Fourier transform infrared spectroscopy and circular dichroism spectroscopy. The possible mechanism of BSA-conjugated PbS nanoparticles growth was also discussed.

  19. Sonocatalytic Damage of Bovine Serum Albumin (BSA) in the Presence of Nanometer Titanium Dioxide (TiO2) Catalyst

    Institute of Scientific and Technical Information of China (English)

    Jun WANG; Jing WU; Zhao Hong ZHANG; Xiang Dong ZHANG; Lei WANG; Liang XU; Bao Dong GUO; Hong LI; Jian TONG

    2005-01-01

    The sonocatalytic damage of bovine serum albumin (BSA) was studied in the presence of nanometer titanium dioxide (TiO2) powders by low frequency (80 kHz) ultrasound. The destruction of secondary structure and change of α-helical structure of BSA were reflected by ultraviolet (UV) and circular dichroism (CD) spectroscopies.

  20. Spectroscopic analysis of the riboflavin-serum albumins interaction on silver nanoparticles

    Energy Technology Data Exchange (ETDEWEB)

    Voicescu, Mariana, E-mail: voicescu@icf.ro; Angelescu, Daniel G. [Institute of Physical Chemistry ' Ilie Murgulescu' , Romanian Academy (Romania); Ionescu, Sorana [University of Bucharest, Department of Physical Chemistry (Romania); Teodorescu, Valentin S. [Institute of Atomic Physics, National Institute of Materials Physics (Romania)

    2013-04-15

    Spectrophotometric behavior of riboflavin (RF) adsorbed on silver nanoparticles as well as its interaction with two serum albumins, BSA and HSA, respectively, has been evidenced. The time evolution of the plasmonic features of the complexes formed by RF/BSA/HSA and Ag(0) nanoparticles having an average diameter of 10.0 {+-} 2.0 nm have been investigated by UV-Vis absorption spectroscopy. Using steady-state and time-resolved fluorescence spectroscopy, the structure, stability, and dynamics of the serum albumins have been studied. The efficiency of energy transfer process between RF and serum albumins on silver nanoparticles has been estimated. A reaction mechanism of RF with silver nanoparticles is also proposed and the results are discussed with relevance to the involvement of the silver nanoparticles to the redox process of RF and to the RF-serum albumins interaction into a silver nanoparticles complex.

  1. Spectroscopic studies on the interaction between ZnSe nanoparticles with bovine serum albumin

    International Nuclear Information System (INIS)

    The interaction between ZnSe nanoparticles (NPs) and bovine serum albumin (BSA) was studied by UV–vis, fluorescence spectroscopic techniques. The results showed that the fluorescence of BSA was strongly quenched by ZnSe NPs and the quenching mechanism was discussed to be a static quenching procedure, which was proved by quenching constant (Kq). The recorded UV–vis data and the fluorescence data quenching by the ZnSe NPs showed that the interaction between them leads to the formation of ZnSe–BSA complex. Based on the synchronous fluorescence spectra, it was established that the conformational change of BSA was induced by the interaction of ZnSe with the tyrosine micro-region of the BSA molecules. Furthermore, the temperature effects on the structural and spectroscopic properties of individual ZnSe NPs and protein and their bioconjugates (ZnSe–BSA) were also researched. It was found that, compared to the monotonic decrease of the individual ZnSe NPs fluorescence intensity, the temperature dependence of the ZnSe–BSA emission had a much more complex behavior, which was highly sensitive to the conformational changes of the protein. - Highlights: ►Interaction between bovine serum albumin (BSA) and ZnSe nanoparticles was studied. ► UV–vis data and fluorescence data demonstrated the formation of ZnSe–BSA complex. ► Temperature dependence of ZnSe–BSA emission was sensitive to the conformational changes of protein.

  2. Albumin-based nanoparticle trehalose lyophilisation stress-down to preserve structure/function and enhanced binding.

    Science.gov (United States)

    Siri, Macarena; Grasselli, Mariano; Alonso, Silvia Del V

    2016-07-15

    The aim of this study was to preserve albumin nanoparticle structure/function during the lyophilisation process. Bovine serum albumin nanoparticles were obtained by γ-irradiation. Nanoparticles were lyophilised in buffer, miliQ water or in trehalose/miliQ solution. The size and charge of the nanoparticles were tested after lyophilisation by light scattering and Z potential. The most relevant results in size of BSA nanoparticle were those lyophilised in PBS between 20 and 350nm, assembled in different aggregates, and negative Z potential obtained was 37±8mV in all, and those nanoparticles lyophilised with trehalose had a size range of 70±2nm and a negative Z potential of 20±5mV. Structure determination of surface aminoacids SH groups in the BSA NP lyophilised in PBS showed an increase in the free SH groups. Different aggregates had different amount of SH groups exposure from 55 to 938 (from smaller to bigger aggregates), whereas BSA NP lyophilised with trehalose showed no significant difference if compared with BSA NP. The binding properties of the BSA nanoparticle with a theragnostic probe (merocyanine 540) were studied after lyophilisation. Results showed more affinity between the BSA NP lyophilised with trehalose than that observed with non lyophilised BSA NP. As a result, the lyophilisation condition in trehalose 100μM solution is the best one to preserve the BSA NP structure/function and the one with the enhance binding affinity of the BSA NP. PMID:27174378

  3. Adsorption of Bovine Serum Albumin (BSA) at the Oil/Water Interface: A Neutron Reflection Study.

    Science.gov (United States)

    Campana, M; Hosking, S L; Petkov, J T; Tucker, I M; Webster, J R P; Zarbakhsh, A; Lu, J R

    2015-05-26

    The structure of the adsorbed protein layer at the oil/water interface is essential to the understanding of the role of proteins in emulsion stabilization, and it is important to glean the mechanistic events of protein adsorption at such buried interfaces. This article reports on a novel experimental methodology for probing protein adsorption at the buried oil/water interface. Neutron reflectivity was used with a carefully selected set of isotopic contrasts to study the adsorption of bovine serum albumin (BSA) at the hexadecane/water interface, and the results were compared to those for the air/water interface. The adsorption isotherm was determined at the isoelectric point, and the results showed that a higher degree of adsorption could be achieved at the more hydrophobic interface. The adsorbed BSA molecules formed a monolayer on the aqueous side of the interface. The molecules in this layer were partially denatured by the presence of oil, and once released from the spatial constraint by the globular framework they were free to establish more favorable interactions with the hydrophobic medium. Thus, a loose layer extending toward the oil phase was clearly observed, resulting in an overall broader interface. By analogy to the air/water interface, as the concentration of BSA increased to 1.0 mg mL(-1) a secondary layer extending toward the aqueous phase was observed, possibly resulting from the steric repulsion upon the saturation of the primary monolayer. Results clearly indicate a more compact arrangement of molecules at the oil/water interface: this must be caused by the loss of the globular structure as a consequence of the denaturing action of the hexadecane. PMID:25875917

  4. Development of morin-conjugated Au nanoparticles: Exploring the interaction efficiency with BSA using spectroscopic methods

    Science.gov (United States)

    Yue, Hua-Li; Hu, Yan-Jun; Huang, Hong-Gui; Jiang, Shan; Tu, Bao

    2014-09-01

    In order to enhance its interaction efficiency with biomacromolecules for the usage as a therapeutic agent, we have conjugated morin, an antioxidant activity and anti-tumor drug, with citrate-coated Au nanoparticles (M-C-AuNPs). M-C-AuNPs were prepared by reducing chloroauric acid using trisodium citrate in the boiling condition, and the resulted M-C-AuNPs were characterized by UV-vis absorption spectroscopy, Transmission Electron Microscopy (TEM), X-ray diffraction (XRD) and FTIR analysis. In this article, UV-vis absorption spectroscopy in combination with fluorescence spectroscopy, and circular dichroism (CD) spectroscopy were employed to investigate the interactions between M-C-AuNPs and bovine serum albumin (BSA), C-AuNPs and BSA in a phosphate buffer at pH 7.4. By comparing the quenching constant KSV, effective quenching constant Ka, binding constant Kb and the number of binding sites n, it is clearly suggested that M-C-AuNPs could enhance the binding force of morin with BSA, which would pave the way for the design of nanotherapeutic agents with improved functionality.

  5. Characterisation of the de-agglomeration effects of bovine serum albumin on nanoparticles in aqueous suspension.

    Science.gov (United States)

    Tantra, Ratna; Tompkins, Jordan; Quincey, Paul

    2010-01-01

    This paper describes the use of nanoparticle characterisation tools to evaluate the interaction between bovine serum albumin (BSA) and dispersed nanoparticles in aqueous media. Dynamic light scattering, zeta-potential measurements and scanning electron microscopy were used to probe the state of zinc oxide (ZnO) and titanium dioxide (TiO(2)) nanoparticles in the presence of various concentrations of BSA, throughout a three-day period. BSA was shown to adhere to ZnO but not to TiO(2). The adsorption of BSA led to subsequent de-agglomeration of the sub-micron ZnO clusters into smaller fragments, even breaking them up into individual isolated nanoparticles. We propose that certain factors, such as adsorption kinetics of BSA on to the surface of ZnO, as well as the initial agglomerated state of the ZnO, prior to BSA addition, are responsible for promoting the de-agglomeration process. Hence, in the case of TiO(2) we see no de-agglomeration because: (a) the nanoparticles are more highly agglomerated to begin with and (b) BSA does not adsorb effectively on the surface of the nanoparticles. The zeta-potential results show that, for either ZnO or TiO(2), the presence of BSA resulted in enhanced stability. In the case of ZnO, the enhanced stability is limited to BSA concentrations below 0.5 wt.%. Steric and electrostatic repulsion are thought to be responsible for improved stability of the dispersion. PMID:19775871

  6. Paclitaxel Albumin-stabilized Nanoparticle Formulation

    Science.gov (United States)

    This page contains brief information about paclitaxel albumin-stabilized nanoparticle formulation and a collection of links to more information about the use of this drug, research results, and ongoing clinical trials.

  7. Novel polyelectrolyte carboxymethyl konjac glucomannan-chitosan nanoparticles for drug delivery. II. Release of albumin in vitro.

    Science.gov (United States)

    Du, Jian; Zhang, Sheng; Sun, Rui; Zhang, Li-Fang; Xiong, Cheng-Dong; Peng, Yu-Xing

    2005-02-15

    Carboxymethyl konjac glucomannan-chitosan (CKGM-CS) nanoparticles were spontaneously prepared under very mild conditions via polyelectrolyte complexation. Bovine serum albumin (BSA), as a model protein drug, was incorporated into the CKGM-CS nanoparticles. The physicochemical properties of the BSA-loaded nanoparticles were identified by Zetasizer 3000 and FTIR spectrophotometry. Their sizes were from 330 nm to 900 nm; zeta potentials were positive according to varies CKGM/CS ratios. The encapsulation efficiency was up 20%. The release behavior in vitro of BSA from the nanoparticles was also investigated. We could find that the BSA release from the CKGM-CS nanoparticles is much more influenced by the CS coating layer than by the CKGM inner structure. And the CKGM-CS matrices not only exhibited pH-responsive properties, but ionic strength-sensitive properties. These systems may present a potential for pulsatile protein drug delivery. PMID:15529331

  8. Study on the binding of colloidal zinc oxide nanoparticles with bovine serum albumin

    Science.gov (United States)

    Kathiravan, A.; Paramaguru, G.; Renganathan, R.

    2009-09-01

    The interaction between colloidal zinc oxide (ZnO) nanoparticles and bovine serum albumin (BSA) was studied by using absorption, fluorescence, Fourier transform infrared, synchronous and time resolved fluorescence spectroscopic measurements. The apparent association constant has been deduced ( Kapp = 1.1 × 10 4 M -1) from the absorption spectral changes of BSA-colloidal ZnO nanoparticles using Benesi-Hildebrand equation. Addition of colloidal ZnO nanoparticles effectively quenched the intrinsic fluorescence of BSA. The number of binding sites ( n = 1.06) and apparent binding constant ( K = 2.5 × 10 4 M -1) were calculated by relevant fluorescence data. Based on Forster's non-radiation energy transfer theory, distance between the donor (BSA) and acceptor (ZnO) ( r0 = 2.88 nm) as well as the critical energy transfer distance ( R0 = 2.49 nm) has also been calculated. The interaction between colloidal ZnO and BSA occurs through static quenching mechanism. The effect of colloidal ZnO nanoparticles on the conformation of BSA has been analyzed by means of UV-visible absorption spectra and synchronous fluorescence spectra.

  9. Gold nanoparticles synthesized by gamma radiation and stabilized by bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Leal, Jessica; Silva, Andressa A.; Geraldes, Adriana N.; Lugao, Ademar B., E-mail: jessicaleal@usp.br [Instituto de Pesquisas Energeticas e Nucleares (IPEN/CNEN-SP), Sao Paulo, SP (Brazil); Grasselli, Mariano, E-mail: mariano.grasselli@gmail.com [Departamento de Ciencia y Tecnologia, Universidad Nacional de Quilmes, Bernal (Argentina)

    2015-07-01

    Gold nanoparticles (AuNPs) are a new option for pharmaceutical and cosmetic industries due to their interesting chemical, electrical and catalytic properties. Research for cancer treatments have been developed using this promising radiotherapy agent. The challenge of gold nanoparticles is to keep them stable, due to metallic behavior. It is know that surface plasma resonance promotes agglomeration of metallic nanoparticles, but they are not stable. Stabilizers have been used to reduce agglomeration. The aim of this work is reduction of HAuCl{sub 4} salt to AuNPs performed by gamma radiation {sup 60}Co source and the stabilization of gold nanoparticles using bovine serum albumin (BSA) fraction V as stabilizer agent. AuNPs were characterized by UV-visible to verify the nanoparticles formation. Samples containing BSA and samples obtained by the conventional method (without stabilizer) were monitored for two weeks and analyzed. Results were compared. (author)

  10. Investigating the influence of effective parameters on molecular characteristics of bovine serum albumin nanoparticles

    Energy Technology Data Exchange (ETDEWEB)

    Rohiwal, S.S.; Satvekar, R.K.; Tiwari, A.P.; Raut, A.V.; Kumbhar, S.G.; Pawar, S.H., E-mail: pawar_s_h@yahoo.com

    2015-04-15

    Graphical abstract: The physiochemical properties of nanoparticles provide the basic aspects about the conformational transitions which could have a strong bearing on the bioavailability for bioactive molecules such as peptides and hormones. - Highlights: • Synthesis and surface and structural properties of Bovine Serum Albumin nanoparticles (BSANPs). • Study of conformational transitions of BSANPs by spectroscopic techniques. • Studies on the effect of pH and protein concentration on formulation of BSANPs. - Abstract: The protein nanoparticles formulation is a challenging task as they are prone to undergo conformational transitions while processing which may affect bioavailability for bioactive compounds. Herein, a modified desolvation method is employed to prepare Bovine Serum Albumin nanoparticles, with controllable particle size ranging from 100 to 300 nm and low polydispersity index. The factors influencing the size and structure of BSA NPs viz. protein concentration, pH and the conditions for purification are well investigated. The structure of BSA NPs is altered due to processing, and may affect the effective binding ability with drugs and bioactive compounds. With that aims, investigations of molecular characteristics of BSA NPs are carried out in detail by using spectroscopic techniques. UV–visible absorption and Fourier Transform Infrared demonstrate the alteration in protein structure of BSA NPs whereas the FT-Raman spectroscopy investigates changes in the secondary and tertiary structures of the protein. The conformational changes of BSA NPs are observed by change in fluorescence intensity and emission maximum wavelength of tryptophan residue by fluorescence spectroscopy. The field emission scanning electron and atomic force microscopy micrographs confirm the size and semi-spherical morphology of the BSA NPs. The effect of concentration and pH on particle size distribution is studied by particle size analyzer.

  11. Investigating the influence of effective parameters on molecular characteristics of bovine serum albumin nanoparticles

    International Nuclear Information System (INIS)

    Graphical abstract: The physiochemical properties of nanoparticles provide the basic aspects about the conformational transitions which could have a strong bearing on the bioavailability for bioactive molecules such as peptides and hormones. - Highlights: • Synthesis and surface and structural properties of Bovine Serum Albumin nanoparticles (BSANPs). • Study of conformational transitions of BSANPs by spectroscopic techniques. • Studies on the effect of pH and protein concentration on formulation of BSANPs. - Abstract: The protein nanoparticles formulation is a challenging task as they are prone to undergo conformational transitions while processing which may affect bioavailability for bioactive compounds. Herein, a modified desolvation method is employed to prepare Bovine Serum Albumin nanoparticles, with controllable particle size ranging from 100 to 300 nm and low polydispersity index. The factors influencing the size and structure of BSA NPs viz. protein concentration, pH and the conditions for purification are well investigated. The structure of BSA NPs is altered due to processing, and may affect the effective binding ability with drugs and bioactive compounds. With that aims, investigations of molecular characteristics of BSA NPs are carried out in detail by using spectroscopic techniques. UV–visible absorption and Fourier Transform Infrared demonstrate the alteration in protein structure of BSA NPs whereas the FT-Raman spectroscopy investigates changes in the secondary and tertiary structures of the protein. The conformational changes of BSA NPs are observed by change in fluorescence intensity and emission maximum wavelength of tryptophan residue by fluorescence spectroscopy. The field emission scanning electron and atomic force microscopy micrographs confirm the size and semi-spherical morphology of the BSA NPs. The effect of concentration and pH on particle size distribution is studied by particle size analyzer

  12. Force spectroscopy with BSA functionalized cantilevers on TiO{sub 2} nanoparticles

    Energy Technology Data Exchange (ETDEWEB)

    Schaefer, Jens; Marxer, Elena Eva Julianne; Bakowsky, Udo [Department of Pharmaceutics, Philipps-Universitaet Marburg, Ketzerbach 63, 35037 Marburg (Germany)

    2011-06-15

    The contact of nanoparticle surfaces with biomolecules often results in interactions. Proteins as one of the most important biomolecules adsorb on nanoparticle surfaces and can affect the way of recognition or of uptake in the cell. Even inhaled nanoparticles can be found on the luminal side of airways and alveoli, major lung tissue compartment or cells and within capillaries. They cross the cell membrane not by endocytotic processes, but by diffusion or adhesive interactions. Due to the possible interaction after inhalative exposure of inorganic nanoparticles with blood biomolecules we investigated the adhesion properties between different TiO{sub 2} nanoparticles and commercial silicon or BSA (as a model protein) modified cantilevers with atomic force microscopy (AFM). The characterization of the nanoparticles was done using laser doppler electrophoresis (LDE), dynamic light scattering (DLS) and transmission electron microscopy (TEM) for zeta potential and size. AFM was used to perform force measurements with unmodified tips and BSA functionalized tips. Adhesion measurements showed differences between the inorganic nanoparticles, regarding their ability to interact with the major serum compound BSA. Scheme of the adhesion measurements on TiO{sub 2} nanoparticles performed with unmodified and BSA modified cantilevers. (Copyright copyright 2011 WILEY-VCH Verlag GmbH and Co. KGaA, Weinheim)

  13. Microwave-assisted synthesis of BSA-modified silver nanoparticles as a selective fluorescent probe for detection and cellular imaging of cadmium(II)

    International Nuclear Information System (INIS)

    We have developed a microwave-assisted method for the synthesis of silver nanoparticles (AgNPs) whose surface is modified with bovine serum albumin (BSA). The reaction involves reduction of the BSA-Ag(I) complex by tyrosine in strongly alkaline solution to form BSA-AgNPs. The reaction takes a few minutes only owing to rapid and uniform microwave heating. The modified AgNPs were characterized by UV–vis and fluorescence spectroscopy, transmission electron microscopy and X- ray photoelectron spectroscopy. The BSA-AgNPs are yellow and display luminescence with a maximum at 521 nm if excited at 465 nm. They have a hydrodynamic diameter of 3–5 nm and possess good colloidal stability in the pH 4.6 to 12.0 range. The fluorescence of the BSA-AgNPs is enhanced by Cd(II) ion due to the formation of a stable hybrid conjugate referred to as Cd-BSA-AgNPs. The effect was exploited to quantify Cd(II) in spiked real water samples with a 4.7 nM detection limit, and also to fluorescently image Cd(II) in Hepatoma cells. (author)

  14. Photophysical studies on the interaction of amides with Bovine Serum Albumin (BSA) in aqueous solution: Fluorescence quenching and protein unfolding

    Energy Technology Data Exchange (ETDEWEB)

    Kumaran, R., E-mail: kumaranwau@rediffmail.com [Department of Chemistry, Dwaraka Doss Goverdhan Doss Vaishnav College, Arumbakkam, Chennai 600106 (India); Ramamurthy, P. [National Centre for Ultrafast Processes, University of Madras, Sekhizar Campus, Taramani, Chennai 600113 (India)

    2014-04-15

    Addition. of amides containing a H-CO(NH{sub 2}) or CH{sub 3}-CO(NH{sub 2}) framework to BSA results in a fluorescence quenching. On the contrary, fluorescence enhancement with a shift in the emission maximum towards the blue region is observed on the addition of dimethylformamide (DMF) (H-CON(CH{sub 3}){sub 2}). Fluorescence quenching accompanied initially with a shift towards the blue region and a subsequent red shift in the emission maximum of BSA is observed on the addition of formamide (H-CO(NH{sub 2})), whereas a shift in the emission maximum only towards the red region results on the addition of acetamide (CH{sub 3}-CONH{sub 2}). Steady state emission spectral studies reveal that amides that possess a free NH{sub 2} and N(CH{sub 3}){sub 2} moiety result in fluorescence quenching and enhancement of BSA respectively. The 3D contour spectral studies of BSA with formamide exhibit a shift in the emission towards the red region accompanied with fluorescence quenching, which indicates that the tryptophan residues of the BSA are exposed to a more polar environment. Circular Dichroism (CD) studies of BSA with amides resulted in a gradual decrease in the α-helical content of BSA at 208 nm, which confirms that there is a conformational change in the native structure of BSA. Time-resolved fluorescence studies illustrate that the extent of buried trytophan moieties exposed to the aqueous phase on the addition of amides follows the order DMFBSA. The fact that the –NH{sub 2} hydrogen and the carbonyl oxygen of amide form a concerted hydrogen-bonding network with the carbonyl oxygen and the amino moieties of amino acids respectively is established from fluorescence methods. -- Highlights:

  15. Irradiation as an alternative route for protein crosslinking: Cosolvent free BSA nanoparticles

    Science.gov (United States)

    Varca, Gustavo H. C.; Queiroz, Rodrigo G.; Lugão, Ademar B.

    2016-07-01

    Recent studies reported the development of protein-based nanoparticles by the use of ɣ-irradiation for the production of advanced drug carriers and biomaterials at nanolevel. Basically, the technique combines protein aggregation by means of protein desolvation using a cosolvent, followed by crosslinking using irradiation. We hereby report the effect irradiation dose over the development of protein-based nanoparticles combined or not with cosolvents. BSA was used as a model protein and the samples were irradiated in phosphate buffer (pH=7.2) using a gammacell in absence or presence of ethanol or methanol at 30% and 40% (v/v) respectively. The irradiation dose effect was evaluated following the exposition of BSA to 2.5, 5, 7.5 and 10 kGy over particle size and protein crosslinking, as determined by photon correlation microscopy and fluorescence measurements. Optimized effects were achieved at 10 kGy, under the assayed dose range, with regard to higher particle size and protein crosslinking levels. The use of irradiation was suitable for the synthesis of BSA nanoparticles and tuning of particle size was achieved by controlling the absorbed dose. While the use of ethanol provided an additional control over BSA particle size if compared to the use of methanol at the concentrations assayed, the possibility to perform BSA crosslinking in absence of cosolvents unraveled a novel one-step procedure for the synthesis of protein nanoparticles with no toxicity generated by the use of cosolvents or monomers.

  16. Glutaraldehyde mediated conjugation of amino-coated magnetic nanoparticles with albumin protein for nanothermotherapy.

    Science.gov (United States)

    Zhao, Lingyun; Yang, Bing; Dai, Xiaochen; Wang, Xiaowen; Gao, Fuping; Zhang, Xiaodong; Tang, Jintian

    2010-11-01

    A novel bioconjugation of amino saline capped Fe3O4 magnetic nanoparticles (MNPs) with bovine serum albumin (BSA) was developed by applying glutaraldehyde as activator. Briefly, Fe3O4 MNs were synthesized by the chemical co-precipitation method. Surface modification of the prepared MNPs was performed by employing amino saline as the coating agent. Glutaraldehyde was further applied as an activation agent through which BSA was conjugated to the amino-coated MNPs. The structure of the BSA-MNs was confirmed by FTIR analysis. Physico-chemical characterizations of the BSA-MNPs, such as surface morphology, surface charge and magnetic properties were investigated by Transmission Electron Microscopy (TEM), zeta-Potential and Vibrating Sample Magnetometer (VSM), etc. Magnetic inductive heating characteristics of the BSA-MNPs were analyzed by exposing the MNPs suspension (magnetic fluid) under alternative magnetic field (AMF). The results demonstrate that BSA was successfully conjugated with amino-coated MNs mediated through glutaraldehyde activation. The nanoparticles were spherical shaped with approximately 10 nm diameter. Possessing ideal magnetic inductive heating characteristics, which can generate very rapid and efficient heating while upon AMF exposure, BSA-MNPs can be applied as a novel candidature for magnetic nanothermotherapy for cancer treatment. In vitro cytotoxicity study on the human hepatocellular liver carcinoma cells (HepG-2) indicates that BSA-MNP is an efficient agent for cancer nanothermotherapy with satisfied biocompatibility, as rare cytotoxicity was observed in the absence of AMF. Moreover, our investigation provides a methodology for fabrication protein conjugated MNPs, for instance monoclonal antibody conjugated MNPs for targeting cancer nanothermotherapy. PMID:21137877

  17. Interaction of carbon nanoparticles to serum albumin: elucidation of the extent of perturbation of serum albumin conformations and thermodynamical parameters

    Energy Technology Data Exchange (ETDEWEB)

    Mandal, Samir [Molecular and Human Genetics Division, CSIR-Indian Institute of Chemical Biology, Kolkata 700032 (India); Hossain, Maidul [Biophysical Chemistry Laboratory, CSIR-Indian Institute of Chemical Biology, Kolkata 700032 (India); Devi, P. Sujatha [Nano-Structured Materials Division, CSIR-Central Glass and Ceramic Research Institute, Kolkata 700032 (India); Kumar, Gopinatha Suresh [Biophysical Chemistry Laboratory, CSIR-Indian Institute of Chemical Biology, Kolkata 700032 (India); Chaudhuri, Keya, E-mail: keya.chaudhuri@gmail.com [Molecular and Human Genetics Division, CSIR-Indian Institute of Chemical Biology, Kolkata 700032 (India)

    2013-03-15

    Highlights: ► Strong interaction of serum albumins to CNPs and potential toxicity. ► Partial unfolding and alteration of BSA and HSA secondary structure by CNP. ► Significant insight into design of nanoparticles in biomedical applications. -- Abstract: Carbon nanoparticles continuously generated from industries and vehicles due to incomplete combustion of fuels is one of the potent causes of air pollution. The exposure of this polluted air with carbon nanoparticles, introduced into the bloodstream of animals in the course of respiration, motivated us to study their interaction with plasma proteins, bovine serum albumin and human serum albumin. Carbon nanoparticles with very small size and high purity were synthesized by dehydration of D-glucose using concentrated sulphuric acid as dehydrating agent. These were characterized by transmission electron microscopy, atomic force microscopy, X-ray diffraction, Raman spectroscopy, FTIR spectroscopy and UV–visible spectroscopy. Carbon nanoparticles-protein interactions were studied by fluorescence spectroscopy, circular dichroism spectroscopy and isothermal titration calorimetry. The fluorescence quenching constants and thermodynamic parameters such as enthalpy change (ΔH°), entropy change (ΔS°) and free energy change (ΔG°) were calculated, which indicated a strong static quenching and primary electrostatic interaction between the carbon nanoparticles and blood proteins. Circular dichroism spectra provided the information about the secondary structure alteration of the proteins in presence of carbon nanoparticles. These findings have shed light towards an understanding of the interactions between carbon nanoparticles and serum proteins which may clarify the potential risks and undesirable health effects of carbon nanoparticles, as well as the related cellular trafficking and systemic translocation.

  18. Interaction of carbon nanoparticles to serum albumin: elucidation of the extent of perturbation of serum albumin conformations and thermodynamical parameters

    International Nuclear Information System (INIS)

    Highlights: ► Strong interaction of serum albumins to CNPs and potential toxicity. ► Partial unfolding and alteration of BSA and HSA secondary structure by CNP. ► Significant insight into design of nanoparticles in biomedical applications. -- Abstract: Carbon nanoparticles continuously generated from industries and vehicles due to incomplete combustion of fuels is one of the potent causes of air pollution. The exposure of this polluted air with carbon nanoparticles, introduced into the bloodstream of animals in the course of respiration, motivated us to study their interaction with plasma proteins, bovine serum albumin and human serum albumin. Carbon nanoparticles with very small size and high purity were synthesized by dehydration of D-glucose using concentrated sulphuric acid as dehydrating agent. These were characterized by transmission electron microscopy, atomic force microscopy, X-ray diffraction, Raman spectroscopy, FTIR spectroscopy and UV–visible spectroscopy. Carbon nanoparticles-protein interactions were studied by fluorescence spectroscopy, circular dichroism spectroscopy and isothermal titration calorimetry. The fluorescence quenching constants and thermodynamic parameters such as enthalpy change (ΔH°), entropy change (ΔS°) and free energy change (ΔG°) were calculated, which indicated a strong static quenching and primary electrostatic interaction between the carbon nanoparticles and blood proteins. Circular dichroism spectra provided the information about the secondary structure alteration of the proteins in presence of carbon nanoparticles. These findings have shed light towards an understanding of the interactions between carbon nanoparticles and serum proteins which may clarify the potential risks and undesirable health effects of carbon nanoparticles, as well as the related cellular trafficking and systemic translocation

  19. Savinase action on bovine serum albumin (BSA) monolayers demonstrated with measurements at the air-water interface and liquid Atomic Force Microscopy (AFM) imaging

    DEFF Research Database (Denmark)

    Balashev, Konstantin; Callisen, Thomas H; Svendsen, Allan; Bjørnholm, Thomas

    2011-01-01

    We studied the enzymatic action of Savinase on bovine serum albumin (BSA) organized in a monolayer spread at the air/water interface or adsorbed at the mica surface. We carried out two types of experiments. In the first one we followed the degradation of the protein monolayer by measuring the...

  20. Good use of fruit wastes: eco-friendly synthesis of silver nanoparticles, characterization, BSA protein binding studies.

    Science.gov (United States)

    Sreekanth, T V M; Ravikumar, Sambandam; Lee, Yong Rok

    2016-06-01

    A simple and eco-friendly methodology for the green synthesis of silver nanoparticles (AgNPs) using a mango seed extract was evaluated. The AgNPs were characterized by ultraviolet-visible spectrophotometry, Fourier transform infrared spectroscopy, transmission electron microscopy, energy dispersive X-ray spectroscopy, and X-ray diffraction. The interaction between the green synthesized AgNPs and bovine serum albumin (BSA) in an aqueous solution at physiological pH was examined by fluorescence spectroscopy. The results confirmed that the AgNPs quenched the fluorophore of BSA by forming a ground state complex in aqueous solution. This fluorescence quenching data were also used to determine the binding sites and binding constants at different temperatures. The calculated thermodynamic parameters (ΔG°, ΔH° and ΔS°) suggest that the binding process occurs spontaneously through the involvement of electrostatic interactions. The synchronous fluorescence spectra showed a blue shift, indicating increasing hydrophobicity. Copyright © 2015 John Wiley & Sons, Ltd. PMID:26644144

  1. nanoparticles via a facile one-step solvothermal process for adsorption of bovine serum albumin

    Science.gov (United States)

    Shen, Mao; Yu, Yujing; Fan, Guodong; Chen, Guang; Jin, Ying min; Tang, Wenyuan; Jia, Wenping

    2014-06-01

    Preparation of magnetic nanoparticles coated with chitosan (CS-coated Fe3O4 NPs) in one step by the solvothermal method in the presence of different amounts of added chitosan is reported here. The magnetic property of the obtained magnetic composite nanoparticles was confirmed by X-ray diffraction (XRD) and magnetic measurements (VSM). Scanning electron microscopy (SEM) and transmission electron microscopy (TEM) allowed the identification of spherical nanoparticles with about 150 nm in average diameter. Characterization of the products by Fourier transform infrared spectroscopy (FTIR) demonstrated that CS-coated Fe3O4 NPs were obtained. Chitosan content in the obtained nanocomposites was estimated by thermogravimetric analysis (TGA). The adsorption properties of the CS-coated Fe3O4 NPs for bovine serum albumin (BSA) were investigated under different concentrations of BSA. Compared with naked Fe3O4 nanoparticles, the CS-coated Fe3O4 NPs showed a higher BSA adsorption capacity (96.5 mg/g) and a fast adsorption rate (45 min) in aqueous solutions. This work demonstrates that the prepared magnetic nanoparticles have promising applications in enzyme and protein immobilization.

  2. Role of hydrogen-bonding and photoinduced electron transfer (PET) on the interaction of resorcinol based acridinedione dyes with Bovine Serum Albumin (BSA) in water

    Energy Technology Data Exchange (ETDEWEB)

    Kumaran, Rajendran, E-mail: kumaranwau@rediffmail.com [Department of Chemistry, Dwaraka Doss Goverdhan Doss, Vaishnav College (Autonomous), 833, Gokul Bagh, E.V.R. Periyar Road, Arumbakkam, Chennai 600106, Tamil Nadu (India); Vanjinathan, Mahalingam [Department of Chemistry, Dwaraka Doss Goverdhan Doss, Vaishnav College (Autonomous), 833, Gokul Bagh, E.V.R. Periyar Road, Arumbakkam, Chennai 600106, Tamil Nadu (India); Ramamurthy, Perumal [National Centre for Ultrafast Processes, University of Madras, Taramani Campus Chennai 600113, Tamil Nadu (India)

    2015-08-15

    Resorcinol based acridinedione (ADDR) dyes are a class of laser dyes and have structural similarity with purine derivatives, nicotinamide adenine dinucleotide (NADH) analogs. These dyes are classified into photoinduced electron transfer (PET) and non-photoinduced electron transfer dyes, and the photophysical properties of family of these dyes exhibiting PET behavior are entirely different from that of non-PET dyes. The PET process in ADDR dyes is governed by the solvent polarity such that an ADDR dye exhibits PET process through space in an aprotic solvent like acetonitrile and does not exhibit the same in protic solvents like water and methanol. A comparison on the fluorescence emission, lifetime and nature of interaction of various ADDR dyes with a large globular protein like Bovine Serum Albumin (BSA) was carried out in aqueous solution. The interaction of PET based ADDR dyes with BSA in water is found to be largely hydrophobic, but hydrogen-bonding interaction of BSA with dye molecule influences the fluorescence emission of the dye and shifts the emission towards red region. Fluorescence spectral studies reveal that the excited state properties of PET based ADDR dyes are largely influenced by the addition of BSA. The microenvironment around the dye results in significant change in the fluorescence lifetime and emission. Fluorescence enhancement with a red shift in the emission results after the addition of BSA to ADDR dyes containing free amino hydrogen in the 10th position of basic acridinedione dye. The amino hydrogen (N–H) in the 10th position of ADDR dye is replaced by methyl group (N–CH{sub 3}), a significant decrease in the fluorescence intensity with no apparent shift in the emission maximum was observed after the addition of BSA. The nature of interaction between ADDR dyes with BSA is hydrogen-bonding and the dye remains unbound even at the highest concentration of BSA. Circular Dichroism (CD) studies show that the addition of dye to BSA results in

  3. Role of hydrogen-bonding and photoinduced electron transfer (PET) on the interaction of resorcinol based acridinedione dyes with Bovine Serum Albumin (BSA) in water

    International Nuclear Information System (INIS)

    Resorcinol based acridinedione (ADDR) dyes are a class of laser dyes and have structural similarity with purine derivatives, nicotinamide adenine dinucleotide (NADH) analogs. These dyes are classified into photoinduced electron transfer (PET) and non-photoinduced electron transfer dyes, and the photophysical properties of family of these dyes exhibiting PET behavior are entirely different from that of non-PET dyes. The PET process in ADDR dyes is governed by the solvent polarity such that an ADDR dye exhibits PET process through space in an aprotic solvent like acetonitrile and does not exhibit the same in protic solvents like water and methanol. A comparison on the fluorescence emission, lifetime and nature of interaction of various ADDR dyes with a large globular protein like Bovine Serum Albumin (BSA) was carried out in aqueous solution. The interaction of PET based ADDR dyes with BSA in water is found to be largely hydrophobic, but hydrogen-bonding interaction of BSA with dye molecule influences the fluorescence emission of the dye and shifts the emission towards red region. Fluorescence spectral studies reveal that the excited state properties of PET based ADDR dyes are largely influenced by the addition of BSA. The microenvironment around the dye results in significant change in the fluorescence lifetime and emission. Fluorescence enhancement with a red shift in the emission results after the addition of BSA to ADDR dyes containing free amino hydrogen in the 10th position of basic acridinedione dye. The amino hydrogen (N–H) in the 10th position of ADDR dye is replaced by methyl group (N–CH3), a significant decrease in the fluorescence intensity with no apparent shift in the emission maximum was observed after the addition of BSA. The nature of interaction between ADDR dyes with BSA is hydrogen-bonding and the dye remains unbound even at the highest concentration of BSA. Circular Dichroism (CD) studies show that the addition of dye to BSA results in a

  4. Bovine serum albumin interacts with silver nanoparticles with a "side-on" or "end on" conformation.

    Science.gov (United States)

    Dasgupta, Nandita; Ranjan, Shivendu; Patra, Dhabaleswar; Srivastava, Priyanka; Kumar, Ashutosh; Ramalingam, Chidambaram

    2016-06-25

    As the nanoparticles (NPs) enter into the biological interface, they have to encounter immediate and first exposure to many proteins of different concentrations. The physicochemical interaction of NPs and proteins is greatly influenced not only by the number and type of proteins; but also the surface chemistry of NPs. To analyze the effects of NPs on proteins, the interaction between bovine serum albumin (BSA) and silver nanoparticles (AgNPs) at different concentrations were investigated. The interaction, BSA conformations, kinetics and adsorption were analyzed by UV-Visible spectrophotometer, dynamic light scattering (DLS), FT-IR spectroscopy and fluorescence quenching. DLS, FTIR and UV-visible spectrophotometric analysis confirms the interaction with minor alterations in size of the protein. Fluorescence quenching analysis confirms the side-on or end-on interaction of 1.5 molecules of BSA to AgNP. Further, pseudo-second order kinetics was determined with equilibrium contact-time of 30 min. The data of the present study determines the detailed evaluation of BSA adsorption on AgNP along with mechanism, kinetics and isotherm of the adsorption. PMID:27180205

  5. Size-dependent interaction of silica nanoparticles with lysozyme and bovine serum albumin proteins

    Science.gov (United States)

    Yadav, Indresh; Aswal, Vinod K.; Kohlbrecher, Joachim

    2016-05-01

    The interaction of three different sized (diameter 10, 18, and 28 nm) anionic silica nanoparticles with two model proteins—cationic lysozyme [molecular weight (MW) 14.7 kDa)] and anionic bovine serum albumin (BSA) (MW 66.4 kDa) has been studied by UV-vis spectroscopy, dynamic light scattering (DLS), and small-angle neutron scattering (SANS). The adsorption behavior of proteins on the nanoparticles, measured by UV-vis spectroscopy, is found to be very different for lysozyme and BSA. Lysozyme adsorbs strongly on the nanoparticles and shows exponential behavior as a function of lysozyme concentration irrespective of the nanoparticle size. The total amount of adsorbed lysozyme, as governed by the surface-to-volume ratio, increases on lowering the size of the nanoparticles for a fixed volume fraction of the nanoparticles. On the other hand, BSA does not show any adsorption for all the different sizes of the nanoparticles. Despite having different interactions, both proteins induce similar phase behavior where the nanoparticle-protein system transforms from one phase (clear) to two phase (turbid) as a function of protein concentration. The phase behavior is modified towards the lower concentrations for both proteins with increasing the nanoparticle size. DLS suggests that the phase behavior arises as a result of the nanoparticles' aggregation on the addition of proteins. The size-dependent modifications in the interaction potential, responsible for the phase behavior, have been determined by SANS data as modeled using the two-Yukawa potential accounting for the repulsive and attractive interactions in the systems. The protein-induced interaction between the nanoparticles is found to be short-range attraction for lysozyme and long-range attraction for BSA. The magnitude of attractive interaction irrespective of protein type is enhanced with increase in the size of the nanoparticles. The total (attractive+repulsive) potential leading to two-phase formation is found to be

  6. Enhanced tumor delivery and antitumor response of doxorubicin-loaded albumin nanoparticles formulated based on a Schiff base.

    Science.gov (United States)

    Li, Fang; Zheng, Chunli; Xin, Junbo; Chen, Fangcheng; Ling, Hua; Sun, Linlin; Webster, Thomas J; Ming, Xin; Liu, Jianping

    2016-01-01

    A novel method was developed here to prepare albumin-based nanoparticles (NPs) for improving the therapeutic and safety profiles of chemotherapeutic agents. This approach involved crosslinking bovine serum albumin (BSA) using a Schiff base-containing vanillin, into NPs and loading doxorubicin (DOX) into the NPs by incubation. The resultant NPs (DOX-BSA-V-NPs) displayed a particle size of 100.5±1.3 nm with a zeta potential of -23.05±1.45 mV and also showed high drug-loading efficiency and excellent stability with respect to storage and temperature. The encapsulation of DOX into the BSA-V-NPs was confirmed by dynamic scanning calorimetry and Raman spectroscopy. DOX-BSA-V-NPs exhibited a significantly faster DOX release at pH 6.5 than pH 7.4, as well as in a solution with a higher glutathione concentration. In vitro studies showed that the cellular uptake of DOX-BSA-V-NPs was time-dependent, concentration-dependent, and faster than free DOX, while the cytotoxicity of DOX-BSA-V-NPs (IC50 value of 3.693 μg/mL) was superior to free DOX (IC50 value of 4.007 μg/mL). More importantly, DOX-BSA-V-NPs showed a longer mean survival time of 24.83 days, a higher tumor inhibition rate of 56.66%, and a decreased distribution in the heart than other DOX formulations in animal studies using a tumor xenograft model. Thus, the vanillin-based albumin NPs were shown here to be a promising carrier for tumor-targeted delivery of chemotherapeutic agents and, thus, should be further studied. PMID:27574421

  7. Enhanced tumor delivery and antitumor response of doxorubicin-loaded albumin nanoparticles formulated based on a Schiff base

    Science.gov (United States)

    Li, Fang; Zheng, Chunli; Xin, Junbo; Chen, Fangcheng; Ling, Hua; Sun, Linlin; Webster, Thomas J; Ming, Xin; Liu, Jianping

    2016-01-01

    A novel method was developed here to prepare albumin-based nanoparticles (NPs) for improving the therapeutic and safety profiles of chemotherapeutic agents. This approach involved crosslinking bovine serum albumin (BSA) using a Schiff base-containing vanillin, into NPs and loading doxorubicin (DOX) into the NPs by incubation. The resultant NPs (DOX-BSA-V-NPs) displayed a particle size of 100.5±1.3 nm with a zeta potential of −23.05±1.45 mV and also showed high drug-loading efficiency and excellent stability with respect to storage and temperature. The encapsulation of DOX into the BSA-V-NPs was confirmed by dynamic scanning calorimetry and Raman spectroscopy. DOX-BSA-V-NPs exhibited a significantly faster DOX release at pH 6.5 than pH 7.4, as well as in a solution with a higher glutathione concentration. In vitro studies showed that the cellular uptake of DOX-BSA-V-NPs was time-dependent, concentration-dependent, and faster than free DOX, while the cytotoxicity of DOX-BSA-V-NPs (IC50 value of 3.693 μg/mL) was superior to free DOX (IC50 value of 4.007 μg/mL). More importantly, DOX-BSA-V-NPs showed a longer mean survival time of 24.83 days, a higher tumor inhibition rate of 56.66%, and a decreased distribution in the heart than other DOX formulations in animal studies using a tumor xenograft model. Thus, the vanillin-based albumin NPs were shown here to be a promising carrier for tumor-targeted delivery of chemotherapeutic agents and, thus, should be further studied. PMID:27574421

  8. Influence of charge on FITC-BSA-loaded chondroitin sulfate-chitosan nanoparticles upon cell uptake in human Caco-2 cell monolayers

    Directory of Open Access Journals (Sweden)

    Hu CS

    2012-09-01

    Full Text Available Chieh-shen Hu,1 Chiao-hsi Chiang,2 Po-da Hong,1,4,* Ming-kung Yeh1–3,*1Biomedical Engineering Program, Graduate Institute of Applied Science and Technology, National Taiwan University of Science and Technology; 2School of Pharmacy, National Defence Medical Center; 3Bureau of Pharmaceutical Affairs, Ministry of National Defence Medical Affairs Bureau; 4Department of Materials Science and Engineering, National Taiwan University of Science and Technology, Taiwan, Republic of China*These authors contributed equally to this workBackground and methods: Chondroitin sulfate-chitosan (ChS-CS nanoparticles and positively and negatively charged fluorescein isothiocyanate-conjugated bovine serum albumin (FITC-BSA-loaded ChS-CS nanoparticles were prepared and characterized. The properties of ChS-CS nanoparticles, including cellular uptake, cytotoxicity, and transepithelial transport, as well as findings on field emission-scanning electron microscopy, transmission electron microscopy, and confocal laser scanning microscopy were evaluated in human epithelial colorectal adenocarcinoma (Caco-2 fibroblasts. ChS-CS nanoparticles with a mean particle size of 250 nm and zeta potentials ranging from –30 to +18 mV were prepared using an ionic gelation method.Results: Standard cell viability assays demonstrated that cells incubated with ChS-CS and FITC-BSA-loaded ChS-CS nanoparticles remained more than 95% viable at particle concentrations up to 0.1 mg/mL. Endocytosis of nanoparticles was confirmed by confocal laser scanning microscopy and measured by flow cytometry. Ex vivo transepithelial transport studies using Caco-2 cells indicated that the nanoparticles were effectively transported into Caco-2 cells via endocytosis. The uptake of positively charged FITC-BSA-loaded ChS-CS nanoparticles across the epithelial membrane was more efficient than that of the negatively charged nanoparticles.Conclusion: The ChS-CS nanoparticles fabricated in this study were

  9. A spectroscopic study on interaction between bovine serum albumin and titanium dioxide nanoparticle synthesized from microwave-assisted hybrid chemical approach.

    Science.gov (United States)

    Ranjan, Shivendu; Dasgupta, Nandita; Srivastava, Priyanka; Ramalingam, Chidambaram

    2016-08-01

    The use of nanoparticles in food or pharma requires a molecular-level perceptive of how NPs interact with protein corona once exposed to a physiological environment. In this study, the conformational changes of bovine serum albumin (BSA) were investigated in detail when exposed to different concentration of titanium dioxide nanoparticle by various techniques. To analyze the effects of NPs on proteins, the interaction between bovine serum albumin and titanium dioxide nanoparticles at different concentrations were investigated. The interaction, BSA conformations, kinetics, and adsorption were analyzed by dynamic light scattering, Fourier transform infrared spectroscopy and fluorescence quenching. Dynamic light scattering analysis confirms the interaction with major changes in the size of the protein. Fluorescence quenching analysis confirms the side-on or end-on interaction of 1.1 molecules of serum albumin to titanium dioxide nanoparticles. Further, pseudo-second order kinetics was determined with equilibrium contact time of 20min. The spectroscopic analysis suggests that there is a conformational change both at secondary and tertiary structure levels. A distortion in both α-helix and β-sheets was observed by Fourier transform infrared (FTIR) spectroscopy. Fluorescence quenching analysis confirms the interaction of a molecule of bovine serum albumin to the single TiO2 nanoparticle. Further, pseudo-second order kinetics was determined with equilibrium contact time of 20min. The data of the present study determines the detailed evaluation of BSA adsorption on TiO2 nanoparticle along with mechanism and adsorption kinetics. PMID:27318604

  10. Adsorption of bovine serum albumin on functionalized silica-coated magnetic MnFe2O4 nanoparticles

    International Nuclear Information System (INIS)

    Two kinds of pH-dependent magnetic nanoadsorbent based on silica-coated MnFe2O4 nanoparticles (SMNPs) and amino-modified silica-coated MnFe2O4 nanoparticles (AS-MNPs) have been synthesized using sol-gel method. X-ray diffraction, Fourier transform infrared spectroscopy and transmission electron microscopy have been employed to characterize the structure and morphology of the nanoadsorbents. The magnetic properties and zeta potential were also investigated. These nanoadsorbents were used to adsorb bovine serum albumin (BSA). The adsorption capacity of BSA largely depended on the pH and ionic strength of solution. In the best result, BSA was adsorbed on AS-MNPs at a high value of 164 mg g-1, which is much higher than that of SMNPs (100 mg g-1). This may due to the increased surface amino that can be conjugated to BSA by a chemical bond and the electrostatic attraction between BSA and magnetic nanoparticles.

  11. Improved activity of immobilized horseradish peroxidase on gold nanoparticles in the presence of bovine serum albumin

    International Nuclear Information System (INIS)

    The using of macromolecular additives is known to be a simple and effective way to improve the activity of immobilized enzymes on solid support, yet the mechanism has not been well understood. Taking horseradish peroxidase (HRP) as an example, only 30 % of its catalytic activity was kept after being immobilized on the surface of 25-nm Au nanoparticles, mainly attributed to the conformational change of the heme-containing active site. The catalytic activity of HRP was significantly improved to 80 % when a certain amount of bovine serum albumin (BSA) was added at the initial stage of the immobilization. Systematic spectral investigation indicated that the addition of BSA inhibited the tertiary structure change around the active site, which was a prerequisite for improved activity of the immobilized HRP. Steady-state kinetic analyses revealed that the introduction of BSA could effectively improve the turnover rate of substrate to product in spite of slight reduced affinity to substrates, which also contributed to the improved catalytic activity

  12. Improved activity of immobilized horseradish peroxidase on gold nanoparticles in the presence of bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Ni, Yuyang; Li, Jun; Huang, Zhenzhen; He, Ke; Zhuang, Jiaqi; Yang, Wensheng, E-mail: wsyang@jlu.edu.cn [Jilin University, State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry (China)

    2013-11-15

    The using of macromolecular additives is known to be a simple and effective way to improve the activity of immobilized enzymes on solid support, yet the mechanism has not been well understood. Taking horseradish peroxidase (HRP) as an example, only 30 % of its catalytic activity was kept after being immobilized on the surface of 25-nm Au nanoparticles, mainly attributed to the conformational change of the heme-containing active site. The catalytic activity of HRP was significantly improved to 80 % when a certain amount of bovine serum albumin (BSA) was added at the initial stage of the immobilization. Systematic spectral investigation indicated that the addition of BSA inhibited the tertiary structure change around the active site, which was a prerequisite for improved activity of the immobilized HRP. Steady-state kinetic analyses revealed that the introduction of BSA could effectively improve the turnover rate of substrate to product in spite of slight reduced affinity to substrates, which also contributed to the improved catalytic activity.

  13. Electrochemical behavior of Ru(H2bpp)2(PF6)2 and its interaction with bovine serum albumin (BSA)

    Institute of Scientific and Technical Information of China (English)

    Qiao Hua Wei; Li Jing Han; Jing Hua Chen; Fang Nan Xiao; Shen Liang Zeng; Guo Nan Chen

    2011-01-01

    In this paper, it was found that Ru(H2bpp)2(PF6)2 (H2bpp = 2,6-bis(pyrazol-3-yl)pyridine) complex had excellent electrochemical activity at the carbon paste electrode in the buffer solution of Tris-HCl (pH 7.0) with a couple reversible redox peaks at 0.296 V and 0.348 V, respectively. Voltammetry was used to investigate the electrochemical behavior of Ru(H2bpp)2(PF6)2 and the interaction between Ru(H2bpp)2(PF6)2 and bovine serum albumin (BSA). In the present of BSA, the oxidation peak current of Ru(H2bpp)2(PF6)2 complex was decreased linearly and the decrease of oxidation peak current of Ru(H2bpp)2(PF6)2 is proportional to BSA concentration from 0.1 to 2.5 mg/L with a detection limit 0.02 mg/L.

  14. Spectroscopic analyses on interaction of Amantadine-Salicylaldehyde, Amantadine-5-Chloro-Salicylaldehyde and Amantadine-o-Vanillin Schiff-Bases with bovine serum albumin (BSA)

    Science.gov (United States)

    Wang, Zhiqiu; Gao, Jingqun; Wang, Jun; Jin, Xudong; Zou, Mingming; Li, Kai; Kang, Pingli

    2011-12-01

    In this work, three Tricyclo [3.3.1.1(3,7)] decane-1-amine (Amantadine) Schiff-Bases, Amantadine-Salicylaldehyde (AS), Amantadine-5-Chloro-Salicylaldehyde (AS-5-C) and Amantadine-o-Vanillin (AS-o-V), were synthesized by direct heating reflux method in ethanol solution and characterized by infrared spectrum and elementary analysis. Fluorescence quenching was used to study the interaction of these Amantadine Schiff-Bases (AS, AS-5-C and AS-o-V) with bovine serum albumin (BSA). According to fluorescence quenching calculations the bimolecular quenching constant ( Kq), apparent quenching constant ( KSV), effective binding constant ( KA) and corresponding dissociation constant ( KD), binding site number ( n) and binding distance ( r) were obtained. The results show that these Amantadine Schiff-Bases can obviously bind to BSA molecules and the binding strength order is AS < AS-5-C = AS-o-V. Synchronous fluorescence spectroscopy reveals that these Amantadine Schiff-Bases adopt different way to bind with BSA molecules. That is, the AS and AS-5-C are accessibility to tryptophan (Trp) residues more than the tyrosine (Tyr) residues, while the AS-o-V is equally close to the Tyr and Trp residues.

  15. Determination of Albumin Using CdS/SiO2 Core/shell Nanoparticles as Fluorescence Probes

    Institute of Scientific and Technical Information of China (English)

    ZHU Changqing; LIU Meigui; WANG Peng; CAO Ming; CAO Chun

    2009-01-01

    CdS quantum dots(QD)were capped with SiO2 via a microemulsion method for reducing the toxicity and imparting the biocompatibility of the CdS QD.The resulting CdS/SiO2 core/shell nanoparticles(NP)showed an improved water-solubility and stability even in pH 4.0 acidic medium.Their fluorescence could be effectively enhanced in the presence of bovine serum albumin(BSA),due to the passivation effect of BSA on the surface of the NP.Furthermore,the concentration dependence of the fluorescence intensity obeys the Langmuir-type binding isotherm.Thus a novel fluorescence enhancement method for the determination of BSA has been developed using the less-toxic CdS/SiO2 core/shell NP as probes.Under optimal conditions,the linear range of calibration curve is 0.6the CdS/SiO2 core/shell NP exhibited slightly lower fluorescence response to BSA as well as other coexisting substances,such as heavy and transition metals,due to the inhibition of SiO2 shell.The proposed method was applied to the quantification of BSA in synthetic and serum samples with satisfactory results.

  16. Inhibitory effect of gold nanoparticles on the D-ribose glycation of bovine serum albumin

    Directory of Open Access Journals (Sweden)

    Liu W

    2014-11-01

    Full Text Available Weixi Liu,1 Menashi A Cohenford,1–3 Leslie Frost,3 Champika Seneviratne,4 Joel A Dain1 1Department of Chemistry, University of Rhode Island, Kingston, RI, USA; 2Department of Integrated Science and Technology, 3Department of Chemistry, Marshall University, Huntington, WV, USA; 4Department of Chemistry, College of the North Atlantic, Labrador, NL, Canada Abstract: Formation of advanced glycation end products (AGEs by nonenzymatic glycation of proteins is a major contributory factor to the pathophysiology of diabetic conditions including senile dementia and atherosclerosis. This study describes the inhibitory effect of gold nanoparticles (GNPs on the D-ribose glycation of bovine serum albumin (BSA. A combination of analytical methods including ultraviolet–visible spectrometry, high performance liquid chromatography, circular dichroism, and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF mass spectrometry were used to determine the extent of BSA glycation in the presence of citrate reduced spherical GNPs of various sizes and concentrations. GNPs of particle diameters ranging from 2 nm to 20 nm inhibited BSA’s AGE formation. The extent of inhibition correlated with the total surface area of the nanoparticles. GNPs of highest total surface area yielded the most inhibition whereas those with the lowest total surface area inhibited the formation of AGEs the least. Additionally, when GNPs’ total surface areas were set the same, their antiglycation activities were similar. This inhibitory effect of GNPs on BSA’s glycation by D-ribose suggests that colloidal particles may have a therapeutic application for the treatment of diabetes and conditions that promote hyperglycemia. Keywords: gold nanoparticles, glycation, AGEs, GNPs, BSA

  17. BSA-conjugated zinc oxide nanoparticles as luminescent probes for the determination of histidine.

    Science.gov (United States)

    Wu, Dudu; Liang, Qiaowen; Chen, Zhi

    2016-06-01

    Zinc oxide nanoparticles doped with bovine serum albumin were used to determine histidine in aqueous solutions using a fluorescence spectroscopic technique. The results showed that histidine effectively quenched the fluorescence of the modified ZnO nanoparticles, whereas other amino acids did not significantly affect the light emission, thereby allowing selective and sensitive histidine detection in amino acid mixtures. Under optimal conditions (pH 7.0, 25 °C, 10 min preincubation), the detection limit for histidine was ~ 9.87 × 10(-7) mol/L. The high value of the determined quenching rate constant Kq (3.30 × 10(13)  L/mol/s) was consistent with a static quenching mechanism. Copyright © 2015 John Wiley & Sons, Ltd. PMID:26577609

  18. Curcumin-incorporated albumin nanoparticles and its tumor image

    Science.gov (United States)

    Gong, Guangming; Pan, Qinqin; Wang, Kaikai; Wu, Rongchun; Sun, Yong; Lu, Ying

    2015-01-01

    Albumin is an ideal carrier for hydrophobic drugs. This paper reports a facile route to develop human serum albumin (HSA)-curcumin (CCM) nanoparticles, in which β-mercaptoethanol (β-ME) acted as an inducer and CCM acted as a bridge. Fluorescence quenching and conformational changes in HSA-CCM nanoparticles occurred during assembly. Disulfide bonds and hydrophobic interactions may play a key role in assembly. HSA-CCM nanoparticles were about 130 nm in size, and the solubility of CCM increased by more than 500 times. The HSA-CCM nanoparticles could accumulate at the cytoplasm of tumor cells and target the tumor tissues. Therefore, HSA nanoparticles fabricated by β-ME denaturation are promising nanocarriers for hydrophobic substances from chemotherapy drugs to imaging probes.

  19. Curcumin-incorporated albumin nanoparticles and its tumor image

    International Nuclear Information System (INIS)

    Albumin is an ideal carrier for hydrophobic drugs. This paper reports a facile route to develop human serum albumin (HSA)–curcumin (CCM) nanoparticles, in which β-mercaptoethanol (β-ME) acted as an inducer and CCM acted as a bridge. Fluorescence quenching and conformational changes in HSA–CCM nanoparticles occurred during assembly. Disulfide bonds and hydrophobic interactions may play a key role in assembly. HSA–CCM nanoparticles were about 130 nm in size, and the solubility of CCM increased by more than 500 times. The HSA–CCM nanoparticles could accumulate at the cytoplasm of tumor cells and target the tumor tissues. Therefore, HSA nanoparticles fabricated by β-ME denaturation are promising nanocarriers for hydrophobic substances from chemotherapy drugs to imaging probes. (paper)

  20. Understanding the Robust Physisorption between Bovine Serum Albumin and Amphiphilic Polymer Coated Nanoparticles.

    Science.gov (United States)

    Liu, Yushuang; Zhong, Ruibo; Zhang, Ping; Ma, Yuxing; Yun, Xiaoling; Gong, Pei; Wei, Jianmin; Zhao, Xinmin; Zhang, Feng

    2016-02-01

    The robust physisorption between nanoparticles (NPs) and proteins has attracted increasing attention due to the significance for both conjugation techniques and protein's corona formation at the bionano interface. In the present study, we first explored the possible binding sites of the bovine serum albumin (BSA) on amphiphilic polymer coated gold nanoparticles (AP-AuNPs). By using mass spectrometry, a 105-amino-acid peptide (12.2 kDa) is discovered as the possible "epitope" responsible for the robust physisorption between BSA and AP-AuNPs. Second, with the help of nanometal surface energy transfer (NSET) theory, we further found that the epitope peptide could insert at least 2.9 nm into the organic molecular layers of AP-AuNPs when the robust conjugates formed, which indicates how such a long epitope peptide can be accommodated by AP-AuNPs and resist protease's digestion. These findings might shed light on a new strategy for studying interactions between proteins and NPs, and further guide the rational design of NPs for safe and effective biomedical applications. PMID:26718324

  1. Effect of the interaction between bovine serum albumin Langmuir monolayer and calcite on the crystallization of CaCO3 nanoparticles

    International Nuclear Information System (INIS)

    Calcium carbonate nanoparticles were generated beneath the Langmuir monolayer of bovine serum albumin (BSA) via templated mineralization. The BSA monolayer and calcium carbonate nanoparticles were characterized based on the measurement of surface pressure-area (π-A) isotherms and area-time curve, and analyses of transmission electron microscopy (TEM), selected area electron diffraction (SAED), scanning electron microscopy (SEM), and X-ray diffraction (XRD) as well. The interaction mechanisms between BSA and calcium carbonate and the role of amorphous calcium carbonate (abridged as ACC) and lattice match in controlling the morphologies and microstructures of the target Calcium carbonate (CaCO3) crystals were discussed, and a model was suggested to illustrate the formation of CaCO3 crystals in the presence of the BSA monolayer. Results indicated that the calcium carbonate nanoparticles were formed through a multi-step process in the presence of the BSA monolayer. Both the amorphous calcium carbonate and lattice match played important roles in terms of the controlled biomineralization and organic matrix-mediated synthesis of CaCO3 nanoparticles. The transformation of amorphous calcium carbonate phase to calcite crystal phase could provide direct evidences to the multistep crystallization process in biomineralization. And the present approach could be used to guide the synthesis of advanced inorganic nanomaterials via simulated biomineralization under mild conditions

  2. Interaction mode and nanoparticle formation of bovine serum albumin and anthocyanin in three buffer solutions

    International Nuclear Information System (INIS)

    Investigation of interaction mode of bovine serum albumin (BSA) and anthocyanin (ACN) in different solutions will help us understand the interaction mechanism and functional change of bioactive small molecule and biomacromolecule. This study investigated the binding mode, including binding constant, number of binding sites, binding force of BSA and ACN interaction in three buffer solutions of phosphate (PBS), sodium chloride (NaCl), and PBS-NaCl, using fluorescence spectroscopy and synchronous fluorescence spectroscopy. Formation and characteristics of BSA–ACN complex were also investigated using dynamic light scattering (DLS) and transmission electron microscopy (TEM). The results showed that ACN could interact with BSA at both tyrosine (Tyr) and tryptophan (Trp) residues through both hydrogen bonds and van der Waals force, and the same binding mode was seen in dH2O and three buffer solutions. The value of binding constant K was decreased as the temperature increased from 298 K to 308 K, and the decreasing degree was in the order of dH2O (9.0×104)>NaCl (2.64×104)/PBS (2.37×104)>PBS-NaCl (0.88×104), which was inversely correlated with the ionic strength of the buffer solutions of PBS-NaCl>NaCl>PBS. It indicated that stability of BSA–ACN complex was affected most in dH2O than in three buffer solutions. The BSA and ACN interaction led to formation of BSA–ACN nanoparticles. The sizes of BSA–ACN nanoparticles in dH2O were smaller than that in three buffer solutions, which correlated with stronger binding force between BSA and ACN in dH2O than in three buffer solutions at room temperature (25 °C, 298 K). - Highlights: • We report the influences of four solutions on the BSA–ACN interaction. • We report the relationship between BSA–ACN interaction and particle size of complex. • The stability of BSA–ACN complex was affected most in dH2O than in buffer solutions

  3. Interaction mode and nanoparticle formation of bovine serum albumin and anthocyanin in three buffer solutions

    Energy Technology Data Exchange (ETDEWEB)

    Zhou, Rui; Dong, Xueyan; Song, Lanlan; Jing, Hao, E-mail: hao.haojing@gmail.com

    2014-11-15

    Investigation of interaction mode of bovine serum albumin (BSA) and anthocyanin (ACN) in different solutions will help us understand the interaction mechanism and functional change of bioactive small molecule and biomacromolecule. This study investigated the binding mode, including binding constant, number of binding sites, binding force of BSA and ACN interaction in three buffer solutions of phosphate (PBS), sodium chloride (NaCl), and PBS-NaCl, using fluorescence spectroscopy and synchronous fluorescence spectroscopy. Formation and characteristics of BSA–ACN complex were also investigated using dynamic light scattering (DLS) and transmission electron microscopy (TEM). The results showed that ACN could interact with BSA at both tyrosine (Tyr) and tryptophan (Trp) residues through both hydrogen bonds and van der Waals force, and the same binding mode was seen in dH{sub 2}O and three buffer solutions. The value of binding constant K was decreased as the temperature increased from 298 K to 308 K, and the decreasing degree was in the order of dH{sub 2}O (9.0×10{sup 4})>NaCl (2.64×10{sup 4})/PBS (2.37×10{sup 4})>PBS-NaCl (0.88×10{sup 4}), which was inversely correlated with the ionic strength of the buffer solutions of PBS-NaCl>NaCl>PBS. It indicated that stability of BSA–ACN complex was affected most in dH{sub 2}O than in three buffer solutions. The BSA and ACN interaction led to formation of BSA–ACN nanoparticles. The sizes of BSA–ACN nanoparticles in dH{sub 2}O were smaller than that in three buffer solutions, which correlated with stronger binding force between BSA and ACN in dH{sub 2}O than in three buffer solutions at room temperature (25 °C, 298 K). - Highlights: • We report the influences of four solutions on the BSA–ACN interaction. • We report the relationship between BSA–ACN interaction and particle size of complex. • The stability of BSA–ACN complex was affected most in dH{sub 2}O than in buffer solutions.

  4. Formation of size and shape tunable gold nanoparticles in solution by bio-assisted synthesis with bovine serum albumin in native and denaturated state

    International Nuclear Information System (INIS)

    Highlights: → We investigate the ability of bovine serum albumin to synthesize gold nanoparticles. → Bovine serum albumin protein acts as both reducing and stabilizing agent. → The size of nanoparticles can be varied by adjusting the protein concentration. → The shape of nanoparticles can be tuned by reaction temperature. → The obtained nanoparticles can be used as bio-substrates for SERS applications. - Abstract: We have successfully controlled the size and shape of gold nanoparticles (GNPs) through a one-step bio-assisted procedure by using bovine serum albumin (BSA) protein as both reducing and stabilizing agent. We found that the growing process of GNPs can be directly manipulated by simply controlling the BSA concentration in solution and the reaction temperature. The GNPs formation was followed both experimentally by UV-vis-NIR spectroscopy and transmission electron microscopy (TEM) and theoretically by finite difference time domain (FDTD) simulations. The surface plasmon resonance of as-prepared GNPs suits the needs of many biological applications.

  5. MULTILAYERS AND POLY(ALLYLAMINE HYDROCHLORIDE)-GRAFT-POLY(ETHYLENE GLYCOL) MODIFIED BOVINE SERUM ALBUMIN NANOPARTICLES: IMPROVED STABILITY AND pH-RESPONSIVE DRUG DELIVERY

    Institute of Scientific and Technical Information of China (English)

    Li-li Xie; Wei-jun Tong; Jian-quan Xu; Chang-you Gao

    2012-01-01

    To improve the colloidal stability of bovine serum albumin (BSA) nanoparticles (NPs) in diverse mediums,poly(allylamine hydrochloride) (PAH)/sodium poly(4-styrene sulfonate) (PSS) multilayers and poly(allylamine hydrochloride)-graft-poly(ethylene glycol) (PAH-g-PEG) coating were coated on the surface of BSA NPs.Stabilities of the BSA NPs in diverse mediums with different surfaces were detected by dynamic light scattering (DLS).Multilayers and PAH-g-PEG coated BSA NPs can be well dispersed in various mediums with a narrow polydispersity index (PDI).The BSA NPs with the highest surface density of PEG show the best stability.The multilayers and PAH-g-PEG coating do not deter the pH-dependent loading and release property of BSA NPs.At pH 9,the encapsulation efficiency of doxorubicin reaches almost 99%,and the release rate at pH 5.5 is significantly higher than that at pH 7.4.

  6. Investigation of interactions between dendrimer-coated magnetite nanoparticles and bovine serum albumin

    International Nuclear Information System (INIS)

    We investigated the interactions between dendrimer-coated magnetite nanoparticles (MNPs) and the protein serum albumin. The investigation was based on the fluorescence quenching of tryptophan residue of serum albumin after binding with the dendrimer-coated magnetite nanoparticles. The extent of the interactions between bovine serum albumin and dendrimer-coated MNPs strongly depends on their surface groups and pH value

  7. Comparison of Calcium Phosphate and Zinc Oxide Nanoparticles as Dermal Penetration Enhancers for Albumin

    OpenAIRE

    Shokri, Narges; Javar, H. A.

    2015-01-01

    Dermal drug delivery is highly preferred by patients due to its several advantages. Protein therapeutics have attracted huge attention recently. Since dermal delivery of proteins encounter problems, in this investigation, zinc oxide nanoparticles and calcium phosphate nanoparticles were compared as enhancers for dermal permeation of albumin. Albumin was applied simultaneously with zinc oxide nanoparticles or calcium phosphate nanoparticles on pieces of mouse skin. Skin permeation of albumin o...

  8. Encapsulation of catechin and epicatechin on BSA NPS improved their stability and antioxidant potential

    OpenAIRE

    Ramdhan, Yadav; Kumar, Dharmesh; Kumari, Avnesh; Sudesh Kumar, Yadav

    2014-01-01

    Nanoencapsulation of antioxidant molecules on protein nanoparticles (NPs) could be an advanced approach for providing stable, better food nutraceuticals and anticancer drugs. The bioavailability and stability of catechin (CAT) and epicatechin (ECAT) were very poor. In the present study, the CAT and ECAT were loaded on bovine serum albumin (BSA) NPs following desolvation method. The transmission electron microscope (TEM) and atomic force microscope (AFM) recorded size of CAT-BSA NPs and ECAT-B...

  9. Spectroscopic analyses on interaction of o-Vanillin- D-Phenylalanine, o-Vanillin- L-Tyrosine and o-Vanillin- L-Levodopa Schiff Bases with bovine serum albumin (BSA)

    Science.gov (United States)

    Gao, Jingqun; Guo, Yuwei; Wang, Jun; Wang, Zhiqiu; Jin, Xudong; Cheng, Chunping; Li, Ying; Li, Kai

    2011-04-01

    In this work, three o-Vanillin Schiff Bases (o-VSB: o-Vanillin- D-Phenylalanine (o-VDP), o-Vanillin- L-Tyrosine (o-VLT) and o-Vanillin- L-Levodopa (o-VLL)) with alanine constituent were synthesized by direct reflux method in ethanol solution, and then were used to study the interaction to bovine serum albumin (BSA) molecules by fluorescence spectroscopy. Based on the fluorescence quenching calculation, the bimolecular quenching constant ( Kq), apparent quenching constant ( Ksv), effective binding constant ( KA) and corresponding dissociation constant ( KD) as well as binding site number ( n) were obtained. In addition, the binding distance ( r) was also calculated according to Foster's non-radioactive energy transfer theory. The results show that these three o-VSB can efficiently bind to BSA molecules, but the binding array order is o-VDP-BSA > o-VLT-BSA > o-VLL-BSA. Synchronous fluorescence spectroscopy indicates that the o-VDP is more accessibility to tryptophan (Trp) residues of BSA molecules than to tyrosine (Tyr) residues. Nevertheless, the o-VLT and o-VLL are more accessibility to Tyr residues than to Trp residues.

  10. Synthesis and characterization of dipicolinate sensitized LaF{sub 3}:Tb{sup 3+} nanoparticles and their interaction with bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Jing, Kui [College of Environment, Liaoning University, Shenyang 110036 (China); Guo, Xingjia, E-mail: guoxja@sina.com [College of Chemistry, Liaoning University, Shenyang 110036 (China); Diao, Xin; Wu, Qiong; Jiang, Yuchun; Sun, Ye; Pan, Xintong; Zhou, Nannan; Zhu, Yanjun [College of Chemistry, Liaoning University, Shenyang 110036 (China)

    2015-01-15

    Dipicolinate sensitized LaF{sub 3}:Tb{sup 3+} luminescent nanoparticles (DPA-NPs) have been successfully synthesized and characterized for their morphology, structural and optical properties. It was found that the prepared DPA-NPs were spherical with an average diameter of 10 nm and their surfaces were capped by citric acid radicals and DPA. And then the interaction between DPA-NPs and bovine serum albumin (BSA) was investigated by fluorescence quenching, UV–visible absorption, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy under the simulative physiological conditions. The results showed that DPA-NPs had a strong ability to quench the intrinsic fluorescence of BSA by forming 1:1 ground-state complexes with a binding constant of about 10{sup 4} L mol{sup −1}. Moreover, the values of the calculated thermodynamic parameters suggested that hydrophobic forces and hydrogen bonds played major roles in stabilizing the complex. The displacement experiments indicated that the binding of DPA-NPs primarily occurred in sub-domain II A (site I) of BSA. The binding distance r was calculated to be 1.9 nm based on the theory of Förster's non-radiation energy transfer. Finally, the analysis of synchronous fluorescence, FT-IR, CD, and three-dimensional fluorescence spectra revealed that the microenvironment of amino acid residues and the conformation of BSA were changed after the addition of DPA-NPs. - Highlights: • Dipicolinate sensitized LaF{sub 3}:Tb{sup 3+} luminescent nanoparticles (DPA-NPs) were synthesized by the hydrothermal method. • DPA-NPs have a strong ability to quench the intrinsic fluorescence of BSA by forming a 1:1 ground state complex. • Hydrophobic force and hydrogen bond played major roles in the binding of DPA-NPs to BSA. • The microenvironment of amino acid residues and the conformation of BSA were changed upon addition of DPA-NPs.

  11. Catalytic formation of silver nanoparticles by bovine serum albumin protected-silver nanoclusters and its application for colorimetric detection of ascorbic acid

    Science.gov (United States)

    Yang, Xiu-Hua; Ling, Jian; Peng, Jun; Cao, Qiu-E.; Wang, Lei; Ding, Zhong-Tao; Xiong, Jie

    2013-04-01

    We established a simple spectrophotometric and colorimetric method for detection of ascorbic acid based on the growth of silver nanoparticles in bovine serum albumin protected-silver nanoclusters (BSA-AgNCs) and Ag+ mixture. Due to the catalysis of BSA-AgNCs, ascorbic acid could reduce Ag+ to silver nanoparticles (NPs) at room temperature. The color of the mixture changed from colorless to yellow and a strong absorption band near 420 nm could be found in their absorption spectra owing to localized surface plasmon resonance (LSPR) of produced silver NPs. The absorbance changes at 420 nm had a good relationship with ascorbic acid concentration. Thus, we proposed a spectrophotometric and colorimetric method to determine ascorbic acid in concentration range from 2.0 to 50.0 μM, with the corresponding limits of determination (3σ) of 0.16 μM.

  12. The synthesis and characterization of monodispersed chitosan-coated Fe3O4 nanoparticles via a facile one-step solvothermal process for adsorption of bovine serum albumin.

    Science.gov (United States)

    Shen, Mao; Yu, Yujing; Fan, Guodong; Chen, Guang; Jin, Ying Min; Tang, Wenyuan; Jia, Wenping

    2014-01-01

    Preparation of magnetic nanoparticles coated with chitosan (CS-coated Fe3O4 NPs) in one step by the solvothermal method in the presence of different amounts of added chitosan is reported here. The magnetic property of the obtained magnetic composite nanoparticles was confirmed by X-ray diffraction (XRD) and magnetic measurements (VSM). Scanning electron microscopy (SEM) and transmission electron microscopy (TEM) allowed the identification of spherical nanoparticles with about 150 nm in average diameter. Characterization of the products by Fourier transform infrared spectroscopy (FTIR) demonstrated that CS-coated Fe3O4 NPs were obtained. Chitosan content in the obtained nanocomposites was estimated by thermogravimetric analysis (TGA). The adsorption properties of the CS-coated Fe3O4 NPs for bovine serum albumin (BSA) were investigated under different concentrations of BSA. Compared with naked Fe3O4 nanoparticles, the CS-coated Fe3O4 NPs showed a higher BSA adsorption capacity (96.5 mg/g) and a fast adsorption rate (45 min) in aqueous solutions. This work demonstrates that the prepared magnetic nanoparticles have promising applications in enzyme and protein immobilization. PMID:24994954

  13. Preparation and characterization of PEG-albumin-curcumin nanoparticles intended to treat breast cancer

    Directory of Open Access Journals (Sweden)

    R Thadakapally

    2016-01-01

    Full Text Available The aim of present research was to prepare novel serum stable long circulating polymeric nanoparticles for curcumin with a modification to the well known and novel nanoparticle albumin bound technology. polyethylene glycol-albumin-curcumin nanoparticles were prepared using serum albumin and poly ethylene glycol using desolvation technique. Nanoparticles were characterized for encapsulation efficiency, particle size and surface morphology. Drug excipient compatibility was determined using fourier transform infrared spectroscopy. Physical state of the drug in the formulations was known by differential scanning colorimetry. In vitrorelease and solubility of the drug from nanoparticles were determined. In vivo Drug release, tissue uptake and kupffer cell uptake was determined with optimized nanoformulation in rats after intravenous administration. Cell viability assay was determined using breast cancer cell line MD-MB-231. Entrapment efficiency for prepared nanoparticle was above 95%. The polyethylene glycol-albumin-curcumin nanoparticles exhibited an interesting release profile with small initial burst followed by slower and controlled release. Solubility of the drug from the formulation was increased. A sustained release of drug from nanoparticles was observed for 35 days in both in vitro and in vivo studies with the optimized formulation. Polyethylene glycol-albumin-curcumin nanoparticles showed lesser liver and kupffer cell uptake as compared to that of curcumin-albumin nanoparticles suggesting the bestowment of stealthness to nanoparticles with pegylation. Also, the antiproliferative activity of polyethylene glycol-albumin-curcumin nanoparticle formulation was more as compared to native curcumin. Polyethylene glycol-albumin-curcumin nanoparticles thus developed can be conveniently used in breast cancer with improved efficacy compared to conventional therapies and as an alternate to nanoparticle albumin bound technology which is used in

  14. BSA Hybrid Synthesized Polymer

    Institute of Scientific and Technical Information of China (English)

    Zong Bin LIU; Xiao Pei DENG; Chang Sheng ZHAO

    2006-01-01

    Bovine serum albumin (BSA), a naturally occurring biopolymer, was regarded as a polymeric material to graft to an acrylic acid (AA)-N-vinyl pyrrolidone (NVP) copolymer to form a biomacromolecular hybrid polymer. The hybrid polymer can be blended with polyethersulfone (PES) to increase the hydrophilicity of the PES membrane, which suggested that the hybrid polymer might have a wide application in the modification of biomaterials.

  15. Investigation of interaction of albumin molecules with diamond nanoparticles in aqueous solutions by dynamic light scattering

    International Nuclear Information System (INIS)

    The method of dynamic light scattering has been used to study the interaction of albumin molecules with diamond nanoparticles in aqueous solutions. It is shown that due to adsorption of albumin on diamond nanoparticles, larger size particles are formed. We have obtained the concentration dependences of the average hydrodynamic radius of these particles. It is found that the carboxylation of the surface of diamond nanoparticles and their pre-coating by albumin leads to a decrease in the adsorption of protein molecules on the surface of nanoparticles and to a decrease in their average hydrodynamic radius. We have also shown that in the range of concentrations of diamond nanoparticles 2-10 μg mL-1, their interaction with albumin molecules at different pH has a different character.

  16. Molecular interactions between some non-steroidal anti-inflammatory drugs (NSAID's) and bovine (BSA) or human (HSA) serum albumin estimated by means of isothermal titration calorimetry (ITC) and frontal analysis capillary electrophoresis (FA/CE).

    Science.gov (United States)

    Ràfols, Clara; Zarza, Sílvia; Bosch, Elisabeth

    2014-12-01

    The interactions between some non-steroidal anti-inflammatory drugs, NSAIDs, (naproxen, ibuprofen and flurbiprofen) and bovine (BSA) or human (HSA) serum albumin have been examined by means of two complementary techniques, isothermal titration calorimetry (ITC) and frontal analysis/capillary electrophoresis (FA/CE). It can be concluded that ITC is able to measure with high precision the strongest drug-albumin interactions but the higher order interactions can be better determined by means of FA/CE. Then, the combination of both techniques leads to a complete evaluation of the binding profiles between the selected NSAIDs and both kind of albumin proteins. When BSA is the binding protein, the NSAIDs show a strong primary interaction (binding constants: 1.5 × 10(7), 8 × 10(5) and 2 × 10(6) M(-1) for naproxen, ibuprofen and flurbiprofen, respectively), and also lower affinity interactions of the same order for the three anti-inflammatories (about 1.7 × 10(4) M(-1)). By contrast, when HSA is the binding protein two consecutive interactions can be observed by ITC for naproxen (9 × 10(5) and 7 × 10(4) M(-1)) and flurbiprofen (5 × 10(6) and 6 × 10(4) M(-1)) whereas only one is shown for ibuprofen (9 × 10(5) M(-1)). Measurements by FA/CE show a single interaction for each drug being the ones of naproxen and flurbiprofen the same that those evaluated by ITC as the second interaction events. Then, the ability of both techniques as suitable complementary tools to establish the whole interaction NSAIDs-albumin profile is experimentally demonstrated and allows foreseeing suitable strategies to establish the complete drug-protein binding profile. In addition, for the interactions analyzed by means of ITC, the thermodynamic signature is established and the relative contributions of the enthalpic and entropic terms discussed. PMID:25159405

  17. Investigation of Bovine Serum Albumin (BSA) Attachment onto Self-Assembled Monolayers (SAMs) Using Combinatorial Quartz Crystal Microbalance with Dissipation (QCM-D) and Spectroscopic Ellipsometry (SE)

    OpenAIRE

    Phan, Hanh T. M.; Bartelt-Hunt, Shannon; Keith B Rodenhausen; Schubert, Mathias; Bartz, Jason C.

    2015-01-01

    Understanding protein adsorption kinetics to surfaces is of importance for various environmental and biomedical applications. Adsorption of bovine serum albumin to various self-assembled monolayer surfaces including neutral and charged hydrophilic and hydrophobic surfaces was investigated using in-situ combinatorial quartz crystal microbalance with dissipation and spectroscopic ellipsometry. Adsorption of bovine serum albumin varied as a function of surface properties, bovine serum albumin co...

  18. Hyaluronic acid-coated bovine serum albumin nanoparticles loaded with brucine as selective nanovectors for intra-articular injection

    Directory of Open Access Journals (Sweden)

    Chen Z

    2013-10-01

    Full Text Available Zhipeng Chen,* Juan Chen,* Li Wu, Weidong Li, Jun Chen, Haibo Cheng, Jinhuo Pan, Baochang CaiDepartment of Pharmacy, Nanjing University of Chinese Medicine, Nanjing, People's Republic of China*These authors contributed equally to this workObjective: To evaluate the potential of hyaluronic acid (HA-coated bovine serum albumin nanoparticles (BSANPs as a novel chondrocyte-targeting drug-delivery nanomedicine.Methods: The HA-BSANPs were characterized by dynamic light scattering, transmission electron microscopy, differential scanning calorimetry, and X-ray diffraction. Fluorescence imaging was used to visualize the distribution of nanoparticles after intra-articular injection. The chondrocyte-targeting efficiency and cellular uptake mechanism of HA-BSANPs were investigated using endocytic inhibitors.Results: HA-BSANPs were successfully prepared with HA coating the surface and amorphous drug in the core. Compared with BSANPs, HA-BSANPs exhibited improved uptake by chondrocytes through a receptor-mediated active uptake mechanism. The endocytosis process of BSANPs and HA-BSANPs involved clathrin-mediated endocytosis, caveolae-mediated endocytosis, and macropinocytosis. No apparent thickening or hyperplasia of the synovium was observed in either BSANPs or HA-BSANPs. The HA-BSANPs could reside in the articular cavity of rats for more than 14 days, which was significantly longer than BSANPs.Conclusion: HA-BSANPs are a promising carrier for articular-related diseases due to elongated articular residence and improved chondrocytic accumulation.Keywords: chondrocyte, intra-articular injection, hyaluronic acid, BSA, nanoparticles

  19. BSA 500 Tutorials / bsa500dotcom

    OpenAIRE

    harryoliver

    2015-01-01

    BSA 500 Entire Course   For more course tutorials visit www.uopbsa500.com   BSA 500 Week 2 Individual Assignment Virtual Organizations Table Part I BSA 500 Week 3 Individual Assignment Table 1 Part 2 Virtual Organization BSA 500 Week 4 Individual Assingment Balance Sheet and Income Statement BSA 500 Week 5 Individual Assignment Financial Ratios Analysis (Riordan Manufacturing) BSA 500 Week 6 Learning Team Assignment Riordan Manufacturing Paper and Pre...

  20. Hysteresis effects of the interaction between serum albumins and silver nanoparticles

    Institute of Scientific and Technical Information of China (English)

    SHEN; Xingcan(沈星灿); YUAN; Qi(袁琦); LIANG; Hong(梁宏); YAN; Haigang(闫海刚); HE; Xiwen(何锡文)

    2003-01-01

    The mechanisms and effects about the interaction between serum albumins and silver nanoparticles have been intensively studied by means of transmission electron microscopy (TEM), circular dichroism (CD) and ultraviolet-visible (UV-Vis) spectroscopy. The adsorption of serum albumins on the surface of silver nanoparticles is observed by TEM. The studies with the surface plasmon bands indicate that the electrostatic and hydrophilic interactions are the major forces between serum albumins and silver nanoparticles; the number of adsorbed monolayer serum albumin molecules to a silver nanoparticle with the size of 60 nm is about 6.7×105. The far-UV CD spectra provide the evidence that the secondary structure of adsorbed serum albumins adopt a looser and more extended conformation, in which the content of α-helix decreases, whereas the content of β-sheet, turn and unordered coil increases. Using time-scanning UV-Vis spectra to monitor the interacting process, the particular twofold hysteresis effects are significantly found with the coverage of aggregated silver nanoparticles and the conformational transition of serum albumins, respectively. The rate constants and the thermodynamics parameters about the hysteretic processes are also calculated.

  1. Interaction of APT with BSA or HSA

    Institute of Scientific and Technical Information of China (English)

    CUI Fengling; CUI Yanrui; LUO Hongxia; YAO Xiaojun; FAN Jing; LU Yan

    2006-01-01

    In this work, N-n-amyl-N'-(sodium p- aminobenzenesulfonate) thiourea (APT) containing saturated fatty hydrocarbon group was synthesized. Fluorescence quenching methods in combination with UV absorption spectra and molecule modeling method were used to study the interaction between APT and bovine serum albumin (BSA) or human serum albumin (HSA). The binding constants of APT with BSA or HSA were determined at different temperatures under the optimum conditions based on the fluorescence quenching results. The binding characteristics of APT and BSA or HSA were reported and the binding sites were obtained. The binding mode was suggested to be mainly hydrophobic interaction, which was consistent with molecular modeling study.

  2. Drug loading and release on tumor cells using silk fibroin–albumin nanoparticles as carriers

    International Nuclear Information System (INIS)

    Polymeric and biodegradable nanoparticles are frequently used in drug delivery systems. In this study silk fibroin–albumin blended nanoparticles were prepared using the desolvation method without any surfactant. These nanoparticles are easily internalized by the cells, reside within perinuclear spaces and act as carriers for delivery of the model drug methotrexate. Methotrexate loaded nanoparticles have better encapsulation efficiency, drug loading ability and less toxicity. The in vitro release behavior of methotrexate from the nanoparticles suggests that about 85% of the drug gets released after 12 days. The encapsulation and loading of a drug would depend on factors such as size, charge and hydrophobicity, which affect drug release. MTT assay and conjugation of particles with FITC demonstrate that the silk fibroin–albumin nanoparticles do not affect the viability and biocompatibility of cells. This blended nanoparticle, therefore, could be a promising nanocarrier for the delivery of drugs and other bioactive molecules. (paper)

  3. Synthesis and characterization of near IR fluorescent albumin nanoparticles for optical detection of colon cancer

    Energy Technology Data Exchange (ETDEWEB)

    Cohen, Sarit; Pellach, Michal [Department of Chemistry, Bar-Ilan Institute of Nanotechnology and Advanced Materials, Bar-Ilan University, Ramat-Gan 52900 (Israel); Kam, Yossi [Institute for Drug Research, School of Pharmacy, Faculty of Medicine, The Hebrew University of Jerusalem, P.O. Box 12065, Jerusalem 91120 (Israel); Grinberg, Igor; Corem-Salkmon, Enav [Department of Chemistry, Bar-Ilan Institute of Nanotechnology and Advanced Materials, Bar-Ilan University, Ramat-Gan 52900 (Israel); Rubinstein, Abraham [Institute for Drug Research, School of Pharmacy, Faculty of Medicine, The Hebrew University of Jerusalem, P.O. Box 12065, Jerusalem 91120 (Israel); Margel, Shlomo, E-mail: shlomo.margel@mail.biu.ac.il [Department of Chemistry, Bar-Ilan Institute of Nanotechnology and Advanced Materials, Bar-Ilan University, Ramat-Gan 52900 (Israel)

    2013-03-01

    Near IR (NIR) fluorescent human serum albumin (HSA) nanoparticles hold great promise as contrast agents for tumor diagnosis. HSA nanoparticles are considered to be biocompatible, non-toxic and non-immunogenic. In addition, NIR fluorescence properties of these nanoparticles are important for in vivo tumor diagnostics, with low autofluorescence and relatively deep penetration of NIR irradiation due to low absorption of biomatrices. The present study describes the synthesis of new NIR fluorescent HSA nanoparticles, by entrapment of a NIR fluorescent dye within the HSA nanoparticles, which also significantly increases the photostability of the dye. Tumor-targeting ligands such as peanut agglutinin (PNA) and anti-carcinoembryonic antigen antibodies (anti-CEA) were covalently conjugated to the NIR fluorescent albumin nanoparticles, increasing the potential fluorescent signal in tumors with upregulated corresponding receptors. Specific colon tumor detection by the NIR fluorescent HSA nanoparticles was demonstrated in a chicken embryo model and a rat model. In future work we also plan to encapsulate cancer drugs such as doxorubicin within the NIR fluorescent HSA nanoparticles for both colon cancer imaging and therapy. - Highlights: Black-Right-Pointing-Pointer Near IR human serum albumin nanoparticles were synthesized and characterized. Black-Right-Pointing-Pointer Nanoparticles were shown to be physically and chemically stable and photostable. Black-Right-Pointing-Pointer Tumor-targeting ligands were covalently conjugated to the nanoparticles. Black-Right-Pointing-Pointer Specific colon cancer tumor detection was demonstrated in chicken-embryo and rat models.

  4. Synthesis and characterization of near IR fluorescent albumin nanoparticles for optical detection of colon cancer

    International Nuclear Information System (INIS)

    Near IR (NIR) fluorescent human serum albumin (HSA) nanoparticles hold great promise as contrast agents for tumor diagnosis. HSA nanoparticles are considered to be biocompatible, non-toxic and non-immunogenic. In addition, NIR fluorescence properties of these nanoparticles are important for in vivo tumor diagnostics, with low autofluorescence and relatively deep penetration of NIR irradiation due to low absorption of biomatrices. The present study describes the synthesis of new NIR fluorescent HSA nanoparticles, by entrapment of a NIR fluorescent dye within the HSA nanoparticles, which also significantly increases the photostability of the dye. Tumor-targeting ligands such as peanut agglutinin (PNA) and anti-carcinoembryonic antigen antibodies (anti-CEA) were covalently conjugated to the NIR fluorescent albumin nanoparticles, increasing the potential fluorescent signal in tumors with upregulated corresponding receptors. Specific colon tumor detection by the NIR fluorescent HSA nanoparticles was demonstrated in a chicken embryo model and a rat model. In future work we also plan to encapsulate cancer drugs such as doxorubicin within the NIR fluorescent HSA nanoparticles for both colon cancer imaging and therapy. - Highlights: ► Near IR human serum albumin nanoparticles were synthesized and characterized. ► Nanoparticles were shown to be physically and chemically stable and photostable. ► Tumor-targeting ligands were covalently conjugated to the nanoparticles. ► Specific colon cancer tumor detection was demonstrated in chicken-embryo and rat models.

  5. Nanoparticles of Conjugated Methotrexate-Human Serum Albumin: Preparation and Cytotoxicity Evaluations

    International Nuclear Information System (INIS)

    Methotrexate-human serum albumin conjugates were developed by a simple carbodiimide reaction. Methotrexate-human serum albumin conjugates were then crosslinked with 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide HCl (EDC) to form nanoparticles. The size of nanoparticles determined by laser light scattering and TEM was between 90 150 nm. Nanoparticles were very stable at physiologic conditions (PBS pH 7.4, 37 degree C) and after incubation with serum. The effect of amount of EDC used for crosslinking on the particle size and free amino groups of nanoparticles was examined. The amount of cross linker showed no significant effect on the size of nanoparticles but free amino groups of nanoparticles were decreased by increasing the cross linker. The physicochemical interactions between methotrexate and human serum albumin were investigated by differential scanning calorimetry (DSC). Nanoparticles were more cytotoxic on T 47 D cells compared to free methotrexate. Moreover, methotrexate-human serum albumin nanoparticles decreased the C50 value of methotrexate on T 47 D cells in comparison with free methotrexate.

  6. Nanoparticles of Conjugated Methotrexate-Human Serum Albumin: Preparation and Cytotoxicity Evaluations

    OpenAIRE

    Azade Taheri; Fatemeh Atyabi; Faranak Salman Nouri; Fatemeh Ahadi; Mohammad Ali Derakhshan; Mohsen Amini; Mohammad Hossein Ghahremani; Seyed Nasser Ostad; Pooria Mansoori; Rassoul Dinarvand

    2011-01-01

    Methotrexate-human serum albumin conjugates were developed by a simple carbodiimide reaction. Methotrexate-human serum albumin conjugates were then crosslinked with 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide HCl (EDC) to form nanoparticles. The size of nanoparticles determined by laser light scattering and TEM was between 90–150 nm. Nanoparticles were very stable at physiologic conditions (PBS pH 7.4, 3 7 ∘ C ) and after incubation with serum. The effect of amount of EDC used for crosslin...

  7. Novel magnetic-fluorescent CS-Fe3O4@ZnS:Mn/ZnS (core/shell) nanoparticles: Preparation, characterization and damage to bovine serum albumin under UV irradiation

    International Nuclear Information System (INIS)

    Novel magnetic-fluorescent nanoparticles (CS-Fe3O4@ZnS:Mn/ZnS) combined ZnS:Mn/ZnS semiconductor nanoparticles and Fe3O4 magnetic nanoparticles with chitosan (CS) matrix were prepared and characterized. Characterization results indicate that CS-Fe3O4@ZnS:Mn/ZnS (core/shell) nanoparticles show superparamagnetic and strong fluorescent properties. Introduction of ZnS shell significantly enhances the photoluminescence intensity by 3.5 times. The saturation magnetization of CS-Fe3O4@ZnS:Mn/ZnS nanoparticles was 14.85 emu g−1 at room temperature. The interaction and damage of CS-Fe3O4@ZnS:Mn/ZnS to bovine serum albumin (BSA) under UV irradiation was investigated by ultraviolet–visible and fluorescence spectra. The results show that electrostatic interaction is the major force for the binding processes of BSA to the surface of CS-Fe3O4@ZnS:Mn/ZnS. The damage of BSA is prone to happen in the presence of CS-Fe3O4@ZnS:Mn/ZnS under UV irradiation. CS-Fe3O4@ZnS:Mn/ZnS may be potential candidate for application as photosensitizers in photodynamic therapy, and fluorescence imaging and magnetic resonance imaging contrast agents for theranostics of cancer. - Highlights: • Novel magnetic-fluorescent CS-Fe3O4@ZnS:Mn/ZnS nanoparticles were synthesized. • CS-Fe3O4@ZnS:Mn/ZnS possesses superparamagnetic and bright fluorescent properties. • Introduction of ZnS shell significantly enhances the PL intensity by 3.5 times. • BSA molecule was effectively damaged by CS-Fe3O4@ZnS:Mn/ZnS under UV irradiation. • Magnetic-fluorescent nanoparticles would be potential agents for cancer treatment

  8. Nanomolar detection of glucose using SERS substrates fabricated with albumin coated gold nanoparticles

    Science.gov (United States)

    Perez-Mayen, Leonardo; Oliva, Jorge; Salas, P.; de La Rosa, Elder

    2016-06-01

    This work presents the design of substrates for Surface Enhanced Raman Scattering (SERS) using star-like gold nanoparticles synthesized by a wet chemical method. The SERS substrates were used for glucose detection for concentrations as low as 10-7 M, which represents an enhancement factor (EF) of 109, as a result of the hot spot formed by the spike termination and appropriate distribution of the gold nanoparticles. An improvement of two orders of magnitude was obtained by coating the gold nanoparticles with albumin with the configuration: glass/Au nanoparticles/albumin. In this case the lowest detection was at a concentration of 10-9 M for an EF of 1011. The albumin molecule allowed us to enhance the Raman signal because of the formation of peptide bonds (COOH-NH2) generated due to the interaction of glucose with albumin, and the appropriate separation distance between the glucose molecules and gold nanoparticles. The presence of such peptide conjugates was confirmed by FTIR spectra. Thus, our results suggest that our SERS substrates can be useful for the detection of very low concentrations of glucose, which is important for the diagnosis of diabetes in the field of medicine.This work presents the design of substrates for Surface Enhanced Raman Scattering (SERS) using star-like gold nanoparticles synthesized by a wet chemical method. The SERS substrates were used for glucose detection for concentrations as low as 10-7 M, which represents an enhancement factor (EF) of 109, as a result of the hot spot formed by the spike termination and appropriate distribution of the gold nanoparticles. An improvement of two orders of magnitude was obtained by coating the gold nanoparticles with albumin with the configuration: glass/Au nanoparticles/albumin. In this case the lowest detection was at a concentration of 10-9 M for an EF of 1011. The albumin molecule allowed us to enhance the Raman signal because of the formation of peptide bonds (COOH-NH2) generated due to the

  9. Photosensitizer-Conjugated Human Serum Albumin Nanoparticles for Effective Photodynamic Therapy

    Directory of Open Access Journals (Sweden)

    Hayoung Jeong, MyungSook Huh, So Jin Lee, Heebeom Koo, Ick Chan Kwon, Seo Young Jeong, Kwangmeyung Kim

    2011-01-01

    Full Text Available Photodynamic therapy (PDT is an emerging theranostic modality for various cancers and diseases. The focus of this study was the development of tumor-targeting albumin nanoparticles containing photosensitizers for efficient PDT. To produce tumor-targeting albumin nanoparticles, the hydrophobic photosensitizer, chlorin e6 (Ce6, was chemically conjugated to human serum albumin (HSA. The conjugates formed self-assembled nanoparticle structures with an average diameter of 88 nm under aqueous conditions. As expected, the Ce6-conjugated HSA nanoparticles (Ce6-HSA-NPs were nontoxic in their native state, but upon illumination with the appropriate wavelength of light, they produced singlet oxygen and damaged target tumor cells in a cell culture system. Importantly, when the nanoparticles were injected through the tail vein into tumor-bearing HT-29 mice, Ce6-HSA-NPs compared with free Ce6 revealed enhanced tumor-specific biodistribution and successful therapeutic results following laser irradiation. These results suggest that highly tumor-specific albumin nanoparticles have the potential to serve not only as efficient therapeutic agents, but also as photodynamic imaging (PDI reagents in cancer treatment.

  10. Surface Modification Of PLGA Nanoparticles Via Human Serum Albumin Conjugation for Controlled Delivery of Docetaxel

    Directory of Open Access Journals (Sweden)

    Saeed Manoochehri

    2013-07-01

    Full Text Available Background:Poly lactic-co-glycolic acid (PLGA based nanoparticles are considered to be a promising drug carrier in tumor targeting but suffer from the high level of opsonization by reticuloendothelial system due to their hydrophobic structure. As a result surface modification of these nanoparticles has been widely studied as an essential step in their development. Among various surface modifications, human serum albumin (HSA possesses advantages including small size, hydrophilic surface and accumulation in leaky vasculature of tumors through passive targeting and a probable active transport into tumor tissues.Methods:PLGA nanoparticles of docetaxel were prepared by emulsification evaporation method and were surface conjugated with human serum albumin. Fourier transform infrared spectrum was used to confirm the conjugation reaction where nuclear magnetic resonance was utilized for conjugation ratio determination. In addition, transmission electron microscopy showed two different contrast media in conjugated nanoparticles. Furthermore, cytotoxicity of free docetaxel, unconjugated and conjugated PLGA nanoparticles was studied in HepG2 cells.Results:Size, zeta potential and drug loading of PLGA nanoparticles were about 199 nm, −11.07 mV, and 4%, respectively where size, zeta potential and drug loading of conjugated nanoparticles were found to be 204 nm, −5.6 mV and 3.6% respectively. Conjugated nanoparticles represented a three-phasic release pattern with a 20% burst effect for docetaxel on the first day. Cytotoxicity experiment showed that the IC50 of HSA conjugated PLGA nanoparticles (5.4 μg was significantly lower than both free docetaxel (20.2 μg and unconjugated PLGA nanoparticles (6.2 μg.Conclusion:In conclusion surface modification of PLGA nanoparticles through HSA conjugation results in more cytotoxicity against tumor cell lines compared with free docetaxel and unconjugated PLGA nanoparticles. Albumin conjugated PLGA nanoparticles may

  11. Engineering of near IR fluorescent albumin nanoparticles for in vivo detection of colon cancer

    Directory of Open Access Journals (Sweden)

    Cohen Sarit

    2012-08-01

    Full Text Available Abstract Background The use of near-infrared (NIR fluorescence imaging techniques has gained great interest for early detection of cancer because water and other intrinsic biomolecules display negligible absorption or autofluorescence in this region. Novel fluorescent nanoparticles with potential to improve neoplasm detection sensitivity may prove to be a valuable tool in early detection of colon tumors. Methods The present study describes the synthesis and use of NIR fluorescent albumin nanoparticles as a diagnostic tool for detection of colon cancer. These fluorescent nanoparticles were prepared by a precipitation process of human serum albumin (HSA in aqueous solution in the presence of a carboxylic acid derivative of the NIR dye IR-783 (CANIR. Tumor-targeting ligands such as peanut agglutinin (PNA, anti-carcinoembryonic antigen antibodies (anti-CEA and tumor associated glycoprotein-72 monoclonal antibodies (anti-TAG-72 were covalently conjugated to the albumin nanoparticles via the surface carboxylate groups by using the carbodiimide activation method. Results and discussion Leakage of the encapsulated dye into PBS containing 4% HSA or human bowel juice was not detected. This study also demonstrates that the encapsulation of the NIR fluorescent dye within the HSA nanoparticles reduces the photobleaching of the dye significantly. Specific colon tumor detection in a mouse model was demonstrated for PNA, anti-CEA and anti-TAG-72 conjugated NIR fluorescent HSA nanoparticles. These bioactive NIR fluorescent albumin nanoparticles also detected invisible tumors that were revealed as pathological only subsequent to histological analysis. Conclusions These results may suggest a significant advantage of NIR fluorescence imaging using NIR fluorescent nanoparticles over regular colonoscopy. In future work we plan to broaden this study by encapsulating cancer drugs, such as paclitaxel and doxorubicin, within these biodegradable NIR fluorescent HSA

  12. Influence of substrate temperature on the properties of pulsed laser deposited silver nanoparticle thin films and their application in SERS detection of bovine serum albumin

    Science.gov (United States)

    Kamakshi, Koppole; Silva, J. P. B.; Sekhar, K. C.; Marslin, Gregory; Moreira, J. Agostinho; Conde, O.; Almeida, A.; Pereira, M.; Gomes, M. J. M.

    2016-05-01

    The effect of substrate temperature ( T s) on electrical conductance, surface plasmon resonance (SPR), and surface-enhanced Raman scattering (SERS) activity of silver nanoparticle (AgNP) thin films is presented. AgNP films are grown on glass substrates by pulsed laser deposition in a controlled Ar atmosphere at a pressure of 0.1 mbar and varying T s. Different T s results in different morphologies, as observed by scanning electron microscopy. The effect of interparticle distance on the electrical conductance of AgNPs is highlighted. The current-voltage characteristics display negative resistance effect and is attributed to the charge trapping process in AgNPs. The film deposited at room temperature presents a SPR peak at λ = 460 nm, and its wavelength first increases until T s reaches 300 °C and then decreases with further increasing T s. The quantitative analysis of SERS studies reveals that SERS intensity of bovine serum albumin (BSA) adsorbed on AgNP substrate deposited at 300 °C exhibits a higher intensity as compared with that of BSA adsorbed on the SERS active substrates at any other T s.

  13. Nanoencapsulation of ultra-small superparamagnetic particles of iron oxide into human serum albumin nanoparticles

    Directory of Open Access Journals (Sweden)

    Matthias G. Wacker

    2014-11-01

    Full Text Available Human serum albumin nanoparticles have been utilized as drug delivery systems for a variety of medical applications. Since ultra-small superparamagnetic particles of iron oxide (USPIO are used as contrast agents in magnetic resonance imaging, their encapsulation into the protein matrix enables the synthesis of diagnostic and theranostic agents by surface modification and co-encapsulation of active pharmaceutical ingredients. The present investigation deals with the surface modification and nanoencapsulation of USPIO into an albumin matrix by using ethanolic desolvation. Particles of narrow size distribution and with a defined particle structure have been achieved.

  14. Bovine Serum Albumin and Chitosan Coated Silver Nanoparticles and Its Antimicrobial Activity against Oral and Nonoral Bacteria

    OpenAIRE

    León Francisco Espinosa-Cristóbal; Gabriel Alejandro Martínez-Castañón; Juan Pablo Loyola-Rodríguez; Nereyda Niño-Martínez; Facundo Ruiz; Norma Verónica Zavala-Alonso; Lara, René H.; Simón Yobanny Reyes-López

    2015-01-01

    Antimicrobial agents have been developed for drug-resistance infections, which have been rapidly increasing; however, the control of involved microorganisms is still a challenge. In this work, SNP with bovine serum albumin (BSA) and chitosan (CS) coatings were prepared with an aqueous reduction method, characterized using dispersion light scattering, transmission electron microscopy, and thermal analysis. Antibacterial activity was tested on seven oral and nonoral bacteria by microdilution te...

  15. Cationic Albumin Nanoparticles for Enhanced Drug Delivery to Treat Breast Cancer: Preparation and In Vitro Assessment

    Directory of Open Access Journals (Sweden)

    Sana Abbasi

    2012-01-01

    Full Text Available Most anticancer drugs are greatly limited by the serious side effects that they cause. Doxorubicin (DOX is an antineoplastic agent, commonly used against breast cancer. However, it may lead to irreversible cardiotoxicity, which could even result in congestive heart failure. In order to avoid these harmful side effects to the patients and to improve the therapeutic efficacy of doxorubicin, we developed DOX-loaded polyethylenimine- (PEI- enhanced human serum albumin (HSA nanoparticles. The formed nanoparticles were ~137 nm in size with a surface zeta potential of ~+15 mV, prepared using 20 μg of PEI added per mg of HSA. Cytotoxicity was not observed with empty PEI-enhanced HSA nanoparticles, formed with low-molecular weight (25 kDa PEI, indicating biocompatibility and safety of the nanoparticle formulation. Under optimized transfection conditions, approximately 80% of cells were transfected with HSA nanoparticles containing tetramethylrhodamine-conjugated bovine serum albumin. Conclusively, PEI-enhanced HSA nanoparticles show potential for developing into an effective carrier for anticancer drugs.

  16. Cationic Albumin Nanoparticles for Enhanced Drug Delivery to Treat Breast Cancer: Preparation and In Vitro Assessment

    OpenAIRE

    Sana Abbasi; Arghya Paul; Wei Shao; Satya Prakash

    2012-01-01

    Most anticancer drugs are greatly limited by the serious side effects that they cause. Doxorubicin (DOX) is an antineoplastic agent, commonly used against breast cancer. However, it may lead to irreversible cardiotoxicity, which could even result in congestive heart failure. In order to avoid these harmful side effects to the patients and to improve the therapeutic efficacy of doxorubicin, we developed DOX-loaded polyethylenimine- (PEI-) enhanced human serum albumin (HSA) nanoparticles. The f...

  17. Ligand Fishing from Dioscorea nipponica Extract Using Human Serum Albumin Functionalized Magnetic Nanoparticles

    OpenAIRE

    Qing, Lin-Sen; Xue, Ying; Zheng, Yi; Xiong, Jing; Liao, Xun; Ding, Li-Sheng; Li, Bo-Gang; Liu, Yi-Ming

    2010-01-01

    Dioscorea nipponica and the preparations made from it have been used for long to prevent and treat coronary heart disease in traditional Chinese medicine. A group of steroidal saponins present in the plant are believed to be the active ingredients. It has been a challenge to study the individual saponins separately due to the similarities in their chemical and physical properties. In this work, human serum albumin (HSA) functionalized magnetic nanoparticles (MNPs) were used to isolate and ide...

  18. Interaction of lipid vesicle with silver nanoparticle-serum albumin protein corona

    OpenAIRE

    Chen, Ran; Choudhary, Poonam; Schurr, Ryan N.; Bhattacharya, Priyanka; Brown, Jared M.; Chun Ke, Pu

    2012-01-01

    The physical interaction between a lipid vesicle and a silver nanoparticle (AgNP)-human serum albumin (HSA) protein “corona” has been examined. Specifically, the binding of AgNPs and HSA was analyzed by spectrophotometry, and the induced conformational changes of the HSA were inferred from circular dichroism spectroscopy. The fluidity of the vesicle, a model system for mimicking cell membrane, was found to increase with the increased exposure to AgNP-HSA corona, though less pronounced compare...

  19. Interaction of lipid vesicle with silver nanoparticle-serum albumin protein corona

    Science.gov (United States)

    Chen, Ran; Choudhary, Poonam; Schurr, Ryan N.; Bhattacharya, Priyanka; Brown, Jared M.; Chun Ke, Pu

    2012-01-01

    The physical interaction between a lipid vesicle and a silver nanoparticle (AgNP)-human serum albumin (HSA) protein "corona" has been examined. Specifically, the binding of AgNPs and HSA was analyzed by spectrophotometry, and the induced conformational changes of the HSA were inferred from circular dichroism spectroscopy. The fluidity of the vesicle, a model system for mimicking cell membrane, was found to increase with the increased exposure to AgNP-HSA corona, though less pronounced compared to that induced by AgNPs alone. This study offers additional information for understanding the role of physical forces in nanoparticle-cell interaction and has implications for nanomedicine and nanotoxicology.

  20. Novel magnetic-fluorescent CS-Fe{sub 3}O{sub 4}@ZnS:Mn/ZnS (core/shell) nanoparticles: Preparation, characterization and damage to bovine serum albumin under UV irradiation

    Energy Technology Data Exchange (ETDEWEB)

    Liu, Li, E-mail: liuli5058@yahoo.cn; Xiao, Ling, E-mail: 775706196@qq.com; Cao, Chunhua

    2013-07-15

    Novel magnetic-fluorescent nanoparticles (CS-Fe{sub 3}O{sub 4}@ZnS:Mn/ZnS) combined ZnS:Mn/ZnS semiconductor nanoparticles and Fe{sub 3}O{sub 4} magnetic nanoparticles with chitosan (CS) matrix were prepared and characterized. Characterization results indicate that CS-Fe{sub 3}O{sub 4}@ZnS:Mn/ZnS (core/shell) nanoparticles show superparamagnetic and strong fluorescent properties. Introduction of ZnS shell significantly enhances the photoluminescence intensity by 3.5 times. The saturation magnetization of CS-Fe{sub 3}O{sub 4}@ZnS:Mn/ZnS nanoparticles was 14.85 emu g{sup −1} at room temperature. The interaction and damage of CS-Fe{sub 3}O{sub 4}@ZnS:Mn/ZnS to bovine serum albumin (BSA) under UV irradiation was investigated by ultraviolet–visible and fluorescence spectra. The results show that electrostatic interaction is the major force for the binding processes of BSA to the surface of CS-Fe{sub 3}O{sub 4}@ZnS:Mn/ZnS. The damage of BSA is prone to happen in the presence of CS-Fe{sub 3}O{sub 4}@ZnS:Mn/ZnS under UV irradiation. CS-Fe{sub 3}O{sub 4}@ZnS:Mn/ZnS may be potential candidate for application as photosensitizers in photodynamic therapy, and fluorescence imaging and magnetic resonance imaging contrast agents for theranostics of cancer. - Highlights: • Novel magnetic-fluorescent CS-Fe{sub 3}O{sub 4}@ZnS:Mn/ZnS nanoparticles were synthesized. • CS-Fe{sub 3}O{sub 4}@ZnS:Mn/ZnS possesses superparamagnetic and bright fluorescent properties. • Introduction of ZnS shell significantly enhances the PL intensity by 3.5 times. • BSA molecule was effectively damaged by CS-Fe{sub 3}O{sub 4}@ZnS:Mn/ZnS under UV irradiation. • Magnetic-fluorescent nanoparticles would be potential agents for cancer treatment.

  1. Templated assembly of albumin-based nanoparticles for simultaneous gene silencing and magnetic resonance imaging

    Science.gov (United States)

    Mertz, Damien; Affolter-Zbaraszczuk, Christine; Barthès, Julien; Cui, Jiwei; Caruso, Frank; Baumert, Thomas F.; Voegel, Jean-Claude; Ogier, Joelle; Meyer, Florent

    2014-09-01

    In this article, we address the design of innovative human serum albumin (HSA)-based nanoparticles loaded with silencing RNA and grafted with gadolinium complexes having average sizes ranging from ca. 50 to 150 nm according to the siRNA/HSA composition. The non-covalent siRNA/HSA assembly is formed on isobutyramide-modified mesoporous silica and the self-supported HSA-based nanoparticles are obtained following the silica template dissolution. These original protein particles provide simultaneous magnetic resonance imaging contrast enhancement and cellular in vitro gene silencing.In this article, we address the design of innovative human serum albumin (HSA)-based nanoparticles loaded with silencing RNA and grafted with gadolinium complexes having average sizes ranging from ca. 50 to 150 nm according to the siRNA/HSA composition. The non-covalent siRNA/HSA assembly is formed on isobutyramide-modified mesoporous silica and the self-supported HSA-based nanoparticles are obtained following the silica template dissolution. These original protein particles provide simultaneous magnetic resonance imaging contrast enhancement and cellular in vitro gene silencing. Electronic supplementary information (ESI) available: Experimental details and supporting Fig. S1-S4. See DOI: 10.1039/c4nr02623c

  2. Bovine Serum Albumin and Chitosan Coated Silver Nanoparticles and Its Antimicrobial Activity against Oral and Nonoral Bacteria

    Directory of Open Access Journals (Sweden)

    León Francisco Espinosa-Cristóbal

    2015-01-01

    Full Text Available Antimicrobial agents have been developed for drug-resistance infections, which have been rapidly increasing; however, the control of involved microorganisms is still a challenge. In this work, SNP with bovine serum albumin (BSA and chitosan (CS coatings were prepared with an aqueous reduction method, characterized using dispersion light scattering, transmission electron microscopy, and thermal analysis. Antibacterial activity was tested on seven oral and nonoral bacteria by microdilution test and scanning electron microscopy. Six different sizes and shapes of coated SNP were prepared and used. Characterization revealed narrow size and good distribution of particles, spherical and pseudospherical shapes, and the presence of coatings on the SNP surfaces. All samples showed antimicrobial activity, although smaller sizes and CS samples had the best inhibition effects. The highest microbial resistance was shown by Gram-positive bacteria. Although coated SNP action depends on particular bacterium, BSA and CS coated SNP could be used for drug-resistance infections.

  3. Preparation and Chiral Selectivity of BSA-Modified Ceramic Membrane

    Institute of Scientific and Technical Information of China (English)

    Cai Lian SU; Rong Ji DAI; Bin TONG; Yu Lin DENG

    2006-01-01

    An affinity-transport system, containing porous ceramic membranes bound with bovine serum albumin (BSA) was used for chiral separation of racemic tryptophan. The preparation of BSA modified ceramic membrane included three steps. Firstly, the membrane was modified with amino group using silanization with an amino silane. Secondly, the amino group modified membrane was bound with aldehyde group using gluteraldehyde. Finally, BSA was covalently bound on the surface of the ceramic membrane. Efficient separation of racemic tryptophan was carried out by performing permeation cell experiments, with BSA modified, porous ceramic membranes.

  4. PEGylated Albumin-Based Polyion Complex Micelles for Protein Delivery.

    Science.gov (United States)

    Jiang, Yanyan; Lu, Hongxu; Chen, Fan; Callari, Manuela; Pourgholami, Mohammad; Morris, David L; Stenzel, Martina H

    2016-03-14

    An increasing amount of therapeutic agents are based on proteins. However, proteins as drug have intrinsic problems such as their low hydrolytic stability. Delivery of proteins using nanoparticles has increasingly been the focus of interest with polyion complex micelles, prepared from charged block copolymer and the oppositely charged protein, as an example of an attractive carrier for proteins. Inspired by this approach, a more biocompatible pathway has been developed here, which replaces the charged synthetic polymer with an abundant protein, such as albumin. Although bovine serum albumin (BSA) was observed to form complexes with positively charged proteins directly, the resulting protein nanoparticle were not stable and aggregated to large precipitates over the course of a day. Therefore, maleimide functionalized poly(oligo (ethylene glycol) methyl ether methacrylate) (MI-POEGMEMA) (Mn = 26000 g/mol) was synthesized to generate a polymer-albumin conjugate, which was able to condense positively charged proteins, here lysozyme (Lyz) as a model. The PEGylated albumin polyion complex micelle with lysozyme led to nanoparticles between 15 and 25 nm in size depending on the BSA to Lyz ratio. The activity of the encapsulated protein was tested using Sprouty 1 (C-12; Spry1) proteins, which can act as an endogenous angiogenesis inhibitor. Condensation of Spry1 with the PEGylated albumin could improve the anticancer efficacy of Spry1 against the breast cancer cells lowering the IC50 value of the protein. Furthermore, the high anticancer efficacy of the POEGMEMA-BSA/Spry1 complex micelle was verified by effectively inhibiting the growth of three-dimensional MCF-7 multicellular tumor spheroids. The PEGylated albumin complex micelle has great potential as a drug delivery vehicle for a new generation of cancer pharmaceuticals. PMID:26809948

  5. Improvement of the Specificity of Surface Plasmon Resonance with BSA-modified Chip

    Institute of Scientific and Technical Information of China (English)

    Li Hua CHEN

    2006-01-01

    A chip was modified with bovine serum albumin (BSA), then interaction between glutathione (GSH) immobilized on the top of BSA and glutathione-S-transferase (GST) was examined, using surface plasmon resonance (SPR). The SPR results showed that BSA-modified chip was effective not only in binding the target proteins but also in suppressing the nonspecific binding (NSB) of proteins.

  6. Interaction of fibrinogen and albumin with titanium dioxide nanoparticles of different crystalline phases

    Science.gov (United States)

    Marucco, Arianna; Fenoglio, Ivana; Turci, Francesco; Fubini, Bice

    2013-04-01

    TiO2 nanoparticles (NPs) are contained in different kinds of industrial products including paints, self-cleaning glasses, sunscreens. TiO2 is also employed in photocatalysis and it has been proposed for waste water treatment. Micrometric TiO2 is generally considered a safe material, while there is concern on the possible health effects of nanometric titania. Due to their small size NPs may migrate within the human body possibly entering in the blood stream. Therefore studies on the interaction of NPs with plasma proteins are needed. In fact, the interaction with proteins is believed to ultimately influences the NPs biological fate. Fibrinogen and albumin are two of the most abundant plasma proteins. They are involved in several important physiological functions. Furthermore, fibrinogen is known to trigger platelet adhesion and inflammation. For these reasons the study of the interaction between these protein and nanoparticles is an important step toward the understanding of the behavior of NPs in the body. In this study we investigated the interaction of albumin and fibrinogen with TiO2 nanoparticles of different crystal phases (rutile and anatase) using an integrated set of techniques. The amount of adsorbed fibrinogen and albumin for each TiO2 surface was investigated by using the bicinchoninic acid assay (BCA). The variation of the surface charge of the NP-protein conjugates respect to the naked NPs was used to indirectly estimate both surface coverage and reversibility of the adsorption upon dilution. Surface charge was monitored by measuring the ζ potential with a conventional electrophoretic light scattering (ELS) system. The extent of protein deformation was evaluated by Raman Spectroscopy. We found that both proteins adsorb irreversibly against electrostatic repulsion, likely undergoing conformational changes or selective orientation upon adsorption. The size of primary particles and the particles aggregation rather than the crystal phase modulate the

  7. Interaction of fibrinogen and albumin with titanium dioxide nanoparticles of different crystalline phases

    International Nuclear Information System (INIS)

    TiO2 nanoparticles (NPs) are contained in different kinds of industrial products including paints, self-cleaning glasses, sunscreens. TiO2 is also employed in photocatalysis and it has been proposed for waste water treatment. Micrometric TiO2 is generally considered a safe material, while there is concern on the possible health effects of nanometric titania. Due to their small size NPs may migrate within the human body possibly entering in the blood stream. Therefore studies on the interaction of NPs with plasma proteins are needed. In fact, the interaction with proteins is believed to ultimately influences the NPs biological fate. Fibrinogen and albumin are two of the most abundant plasma proteins. They are involved in several important physiological functions. Furthermore, fibrinogen is known to trigger platelet adhesion and inflammation. For these reasons the study of the interaction between these protein and nanoparticles is an important step toward the understanding of the behavior of NPs in the body. In this study we investigated the interaction of albumin and fibrinogen with TiO2 nanoparticles of different crystal phases (rutile and anatase) using an integrated set of techniques. The amount of adsorbed fibrinogen and albumin for each TiO2 surface was investigated by using the bicinchoninic acid assay (BCA). The variation of the surface charge of the NP-protein conjugates respect to the naked NPs was used to indirectly estimate both surface coverage and reversibility of the adsorption upon dilution. Surface charge was monitored by measuring the ζ potential with a conventional electrophoretic light scattering (ELS) system. The extent of protein deformation was evaluated by Raman Spectroscopy. We found that both proteins adsorb irreversibly against electrostatic repulsion, likely undergoing conformational changes or selective orientation upon adsorption. The size of primary particles and the particles aggregation rather than the crystal phase modulate the

  8. Nanoparticle Albumin Bound Paclitaxel in the Treatment of Human Cancer: Nanodelivery Reaches Prime-Time?

    Directory of Open Access Journals (Sweden)

    Iole Cucinotto

    2013-01-01

    Full Text Available Nanoparticle albumin bound paclitaxel (nab-paclitaxel represents the first nanotechnology-based drug in cancer treatment. We discuss the development of this innovative compound and report the recent changing-practice results in breast and pancreatic cancer. A ground-breaking finding is the demonstration that nab-paclitaxel can not only enhance the activity and reduce the toxicity of chromophore-diluted compound, but also exert activity in diseases considered refractory to taxane-based treatment. This is the first clinical demonstration of major activity of nanotechnologically modified drugs in the treatment of human neoplasms.

  9. Characteristics of magnetic Fe3O4 nanoparticles encapsulated with human serum albumin

    Institute of Scientific and Technical Information of China (English)

    2006-01-01

    Magnetic nanoparticles (Fe3O4) were prepared by chemical precipitation method using Fe2+ and Fe3+salts with sodium hydroxide in the nitrogen atmosphere. Fe3O4 nanoparticles were coated with human serum albumin(HSA) for magnetic resonance imaging as contrast agent. Characteristics of magnetic particles coated or uncoated were carried out using scanning electron microscopy and X-ray diffraction. Zeta potentials, package effects and distributions of colloid particles were measured to confirm the attachment of HSA on magnetic particles. Effects of Fe3O4 nanoparticles coated with HSA on magnetic resonance imaging were investigated with rats. The experimental results show that the adsorption of HSA on magnetic particles is very favorable to dispersing of magnetic Fe3O4 particles, while the sizes of Fe3O4 particles coated are related to the molar ratio of Fe3O4 to HSA. The diameters of the majority of particles coated are less than 100 nm. Fe3O4 nanoparticle coated with HSA has a good biocompatibility and low toxicity. This new contrast agent has some effects on the nuclear magnetic resonance imaging of liver and the lowest dosage is 20 μmol/kg for the demands of diagnosis.

  10. Synthesis and Applications of Multimodal Hybrid Albumin Nanoparticles for Chemotherapeutic Drug Delivery and Photothermal Therapy Platforms

    Science.gov (United States)

    Peralta, Donna V.

    Progress has been made in using human serum albumin nanoparticles (HSAPs) as carrier systems for targeted treatment of cancer. Human serum albumin (HSA), the most abundant human blood protein, can form HSAPs via a desolvation and crosslinking method, with the size of the HSAPs having crucial importance for drug loading and in vivo performance. Gold nanoparticles have also gained medicinal attention due to their ability to absorb near-infrared (NIR) light. These relatively non-toxic particles offer combinational therapy via imaging and photothermal therapy (PPTT) capabilities. A desolvation and crosslinking approach was employed to encapsulate gold nanoparticles (AuNPs), hollow gold nanoshells (AuNSs), and gold nanorods (AuNRs), into efficiently sized HSAPs for future tumor heat ablation via PPTT. The AuNR-HSAPs, AuNP-HSAPs and AuNS-HSAPs had average particle diameters of 222 +/- 5, 195 +/- 9 and 156 +/- 15, respectively. We simultaneously encapsulated AuNRs and the anticancer drug paclitaxel (PAC), forming PAC-AuNR-HSAPs with overall average particle size of 299 +/- 6 nm. Loading of paclitaxel into PAC-AuNR-HSAPs reached 3microg PAC/mg HSA. PAC-AuNR-HSAPs experienced photothermal heating of 46 °C after 15 minutes of NIR laser exposure; the temperature necessary to cause severe cellular hyperthermia. There was a burst release of paclitaxel up to 188 ng caused by the irradiation session, followed by a temporal drug release. AuNR-HSAPs were tested for ablation of renal cell carcinoma using NIR irradiation in vitro. Particles created with the same amount of AuNRs, but varying HSA (1, 5 or 20 mg) showed overall particle size diameters 409 +/- 224, 294 +/- 83 and 167 +/- 4 nm, respectively. Increasing HSAPs causes more toxicity under non-irradiated treatment conditions: AuNR-HSAPs with 20 mg versus 5 mg HSA caused cell viability of 64.5% versus 87%, respectively. All AuNR-HSAPs batches experienced photothermal heating above 42 °C. Coumarin-6, was used to visualize the

  11. BSA 502 Course tutorial/ indigohelp

    OpenAIRE

    ADGV

    2015-01-01

    For more classes visit www.indigohelp.com   BSA 502 Week 2 Individual Assignment Marketing Issues Paper (Kudler Fine Foods) BSA 502 Week 2 Team Assignment Sales and Marketing Paper (Riordan Manufacturing) BSA 502 Week 3 Individual Assignment Human Resource Paper (Kudler Fine Foods) BSA 502 Week 3 Team Assignment Human Resources Paper ( Riordan Manufacturing) BSA 502 Week 4 Individual Assignment Operations and Logistics Issues (Kudler Fine Foods) BSA 502 We...

  12. BSA 500 Course tutorial/ indigohelp

    OpenAIRE

    ASDVV

    2015-01-01

    For more classes visit www.indigohelp.com   BSA 500 Week 1 Learning Team Charter BSA 500 Week 2 Individual Assignment Virtual Organizations Table Part I BSA 500 week 3 Individual Assignment Table 1 Part 2 Virtual Organization BSA 500 Week 4 Individual Assingment Balance Sheet and Income Statement BSA 500 Week 5 Individual Assignment Financial Ratios Analysis (Riordan Manufacturing) BSA 500 Week 6 Learning Team Assignment Riordan Manufacturing Paper and Pre...

  13. Development of a lauric acid/albumin hybrid iron oxide nanoparticle system with improved biocompatibility.

    Science.gov (United States)

    Zaloga, Jan; Janko, Christina; Nowak, Johannes; Matuszak, Jasmin; Knaup, Sabine; Eberbeck, Dietmar; Tietze, Rainer; Unterweger, Harald; Friedrich, Ralf P; Duerr, Stephan; Heimke-Brinck, Ralph; Baum, Eva; Cicha, Iwona; Dörje, Frank; Odenbach, Stefan; Lyer, Stefan; Lee, Geoffrey; Alexiou, Christoph

    2014-01-01

    The promising potential of superparamagnetic iron oxide nanoparticles (SPIONs) in various nanomedical applications has been frequently reported. However, although many different synthesis methods, coatings, and functionalization techniques have been described, not many core-shell SPION drug delivery systems are available for clinicians at the moment. Here, bovine serum albumin was adsorbed onto lauric acid-stabilized SPIONs. The agglomeration behavior, zeta potential, and their dependence on the synthesis conditions were characterized with dynamic light scattering. The existence and composition of the core-shell-matrix structure was investigated by transmission electron microscopy, Fourier transform infrared spectroscopy, and zeta potential measurements. We showed that the iron oxide cores form agglomerates in the range of 80 nm. Moreover, despite their remarkably low tendency to aggregate even in a complex media like whole blood, the SPIONs still maintained their magnetic properties and were well attractable with a magnet. The magnetic properties were quantified by vibrating sample magnetometry and a superconducting quantum interference device. Using flow cytometry, we further investigated the effects of the different types of nanoparticle coating on morphology, viability, and DNA integrity of Jurkat cells. We showed that by addition of bovine serum albumin, the toxicity of nanoparticles is greatly reduced. We also investigated the effect of the particles on the growth of primary human endothelial cells to further demonstrate the biocompatibility of the particles. As proof of principle, we showed that the hybrid-coated particles are able to carry payloads of up to 800 μg/mL of the cytostatic drug mitoxantrone while still staying colloidally stable. The drug-loaded system exhibited excellent therapeutic potential in vitro, exceeding that of free mitoxantrone. In conclusion, we have synthesized a biocompatible ferrofluid that shows great potential for clinical

  14. Preparation, characterization, and in vitro targeted delivery of folate-decorated paclitaxel-loaded bovine serum albumin nanoparticles

    Directory of Open Access Journals (Sweden)

    Dongmei Zhao

    2010-09-01

    Full Text Available Dongmei Zhao, Xiuhua Zhao, Yuangang Zu, Jialei Li, Yu Zhang, Ru Jiang, Zhonghua ZhangKey Laboratory of Forest Plant Ecology, Northeast Forestry University, Ministry of Education, Harbin, Heilongjiang, ChinaAbstract: Paclitaxel (Taxol® is an important anticancer drug in clinical use for treatment of a variety of cancers. Because of its low solubility, it is formulated in high concentration in Cremophor EL® which induces hypersensitivity reactions. In this study, targeted delivery of paclitaxel-loaded nanoparticles was prepared by a desolvation procedure, crosslinked on the wall material of bovine serum albumin, and subsequently decorated by folic acid. The characteristics of the nanoparticles, such as amount of folate conjugation, surface morphology, drug entrapment efficiency, drug loading efficiency, and release kinetics were investigated in vitro. The targeting effect was investigated in vitro by cancer cell uptake of fluorescein isothiocyanate-labeled nanoparticles. The spherical nanoparticles obtained were negatively charged with a zeta potential of about -30 mV, and characterized around 210 nm with a narrow size distribution. Drug entrapment efficiency and drug loading efficiency were approximately 95.3% and 27.2%, respectively. The amount of folate conjugation was 9.22 µg/mg of bovine serum albumin. The folate-decorated nanoparticles targeted a human prostate cancer cell line effectively.Keywords: paclitaxel, bovine serum albumin, folate, nanoparticles, target delivery

  15. Interaction of Nicotine and Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    2000-01-01

    The binding of nicotine to bovine serum albumin (BSA) was studied by UV absorption, fluorescence, and 1H NMR methods. With the addition of nicotine, the absorption band of BSA at about 210 nm decreased gradually, moved to longer wavelengths, and narrowed. BSA fluorescence of tryptophan residue was quenched by nicotine. The 1H NMR peaks of nicotine moved to downfield by the addition of BSA. The experimental results showed that nicotine was capable of binding with BSA to form a 1:1 complex. BSA's high selectivity for nicotine binding suggests a unique role for this protein in the detoxification and/or transport of nicotine.

  16. Enhanced Cytotoxicity to Cancer Cells by Codelivery and Controlled Release of Paclitaxel-loaded Sirolimus-conjugated Albumin Nanoparticles.

    Science.gov (United States)

    Behrouz, Hossein; Esfandyari-Manesh, Mehdi; Khoeeniha, Mohammad Kazem; Amini, Mohsen; Shiri Varnamkhasti, Behrang; Atyabi, Fatemeh; Dinarvand, Rassoul

    2016-08-01

    Recently, it is suggested that mTOR signaling pathway is an important mediator in many cancers especially breast cancer. Therefore, effects of sirolimus as a mTOR inhibitor in breast cancer have been studied in combination with paclitaxel with or without controlled release effect. In this work, we prepared a water-soluble formulation of sirolimus-conjugated albumin nanoparticles loaded with paclitaxel, to study the effects of sirolimus concentration when it releases more later than paclitaxel in comparison with sirolimus-paclitaxel-loaded albumin nanoparticles. Also effects of paclitaxel loading on cytotoxic properties of nanoparticles were studied. Sirolimus was succinylated at 42-OH with enzymatic reaction of Candida antarctica lipase B, and then its carboxylic group was activated with EDC/NHS and conjugated to the lysine residues of albumin. Paclitaxel was loaded on albumin surface by nab technique in concentration range of 0-10 μg/mL. Sirolimus-conjugated nanoparticles with 0.01 μg/mL paclitaxel showed lowest cell viability of 44% while it was 53% for non-conjugated nanoparticles in MDA-MB-468 cell lines after 48 h (p-value = 0.003). In MCF-7 cell lines, sirolimus-conjugated nanoparticles with 0.1 μg/mL paclitaxel showed lowest cell viability of 35.69% while it was 48% for non-conjugated nanoparticles after 48 h (p-value = 0.03). We guess that when cancer cell lines arrest in G2-M by anticancer drugs like paclitaxel, Akt activates mTOR to make cells continue living, then inhibiting mTOR can enhance anticancer effects. PMID:26913996

  17. Cabazitaxel-loaded human serum albumin nanoparticles as a therapeutic agent against prostate cancer

    Directory of Open Access Journals (Sweden)

    Qu N

    2016-07-01

    Full Text Available Na Qu,1 Robert J Lee,1,2 Yating Sun,1 Guangsheng Cai,1 Junyang Wang,1 Mengqiao Wang,1 Jiahui Lu,1 Qingfan Meng,1 Lirong Teng,1 Di Wang,1 Lesheng Teng1,3 1School of Life Sciences, Jilin University, Changchun, People’s Republic of China; 2Division of Pharmaceutics, College of Pharmacy, The Ohio State University, Columbus, OH, USA; 3State Key Laboratory of Long-acting and Targeting Drug Delivery System, Yantai, People’s Republic of China Abstract: Cabazitaxel-loaded human serum albumin nanoparticles (Cbz-NPs were synthesized to overcome vehicle-related toxicity of current clinical formulation of the drug based on Tween-80 (Cbz-Tween. A salting-out method was used for NP synthesis that avoids the use of chlorinated organic solvent and is simpler compared to the methods based on emulsion-solvent evaporation. Cbz-NPs had a narrow particle size distribution, suitable drug loading content (4.9%, and superior blood biocompatibility based on in vitro hemolysis assay. Blood circulation, tumor uptake, and antitumor activity of Cbz-NPs were assessed in prostatic cancer xenograft-bearing nude mice. Cbz-NPs exhibited prolonged blood circulation and greater accumulation of Cbz in tumors along with reduced toxicity compared to Cbz-Tween. Moreover, hematoxylin and eosin histopathological staining of organs revealed consistent results. The levels of blood urea nitrogen and serum creatinine in drug-treated mice showed that Cbz-NPs were less toxic than Cbz-Tween to the kidneys. In conclusion, Cbz-NPs provide a promising therapeutic for prostate cancer. Keywords: cabazitaxel, human serum albumin, nanoparticle, drug delivery, toxicity, pros­tate cancer

  18. Development of a lauric acid/albumin hybrid iron oxide nanoparticle system with improved biocompatibility

    Directory of Open Access Journals (Sweden)

    Zaloga J

    2014-10-01

    Full Text Available Jan Zaloga,1 Christina Janko,1 Johannes Nowak,2 Jasmin Matuszak,1 Sabine Knaup,1 Dietmar Eberbeck,3 Rainer Tietze,1 Harald Unterweger,1 Ralf P Friedrich,1 Stephan Duerr,1 Ralph Heimke-Brinck,4 Eva Baum,4 Iwona Cicha,1 Frank Dörje,4 Stefan Odenbach,2 Stefan Lyer,1 Geoffrey Lee,5 Christoph Alexiou1 1Department of Otorhinolaryngology, Head and Neck Surgery, Section for Experimental Oncology and Nanomedicine (SEON, Else Kröner-Fresenius-Stiftung-Professorship, University Hospital Erlangen, Erlangen, Germany; 2Measuring and Automation Technology, Technical University Dresden, Dresden, Germany; 3Physikalisch-Technische-Bundesanstalt, Berlin, Germany; 4Pharmacy Department, University Hospital Erlangen, Erlangen, Germany; 5Division of Pharmaceutics, Friedrich Alexander University Erlangen-Nuremberg, Erlangen, Germany Abstract: The promising potential of superparamagnetic iron oxide nanoparticles (SPIONs in various nanomedical applications has been frequently reported. However, although many different synthesis methods, coatings, and functionalization techniques have been described, not many core-shell SPION drug delivery systems are available for clinicians at the moment. Here, bovine serum albumin was adsorbed onto lauric acid-stabilized SPIONs. The agglomeration behavior, zeta potential, and their dependence on the synthesis conditions were characterized with dynamic light scattering. The existence and composition of the core-shell-matrix structure was investigated by transmission electron microscopy, Fourier transform infrared spectroscopy, and zeta potential measurements. We showed that the iron oxide cores form agglomerates in the range of 80 nm. Moreover, despite their remarkably low tendency to aggregate even in a complex media like whole blood, the SPIONs still maintained their magnetic properties and were well attractable with a magnet. The magnetic properties were quantified by vibrating sample magnetometry and a superconducting quantum

  19. BSA 500 Course Tutorial / tutorialrank

    OpenAIRE

    welcome8888

    2015-01-01

    BSA 500 Entire Course (UOP Course) For more course tutorials visit   www.tutorialrank.com   Tutorial Purchased: 4 Times, Rating: A+           BSA 500 Week 1 Learning Team Charter (UOP Course) BSA 500 Week 2 Individual Assignment Virtual Organizations Table Part I (UOP Course) BSA 500 Week 3 Individual Assignment Table 1 Part 2 Virtual Organization (UOP Course) BSA 500 Week 4 Individual Assingment Balanc...

  20. Preparation of 10-hydroxycamptothecin-loaded glycyrrhizic acid-conjugated bovine serum albumin nanoparticles for hepatocellular carcinoma-targeted drug delivery

    OpenAIRE

    Zu Y; Meng L; Zhao X; Ge Y.; Yu X.; Zhang Y; Deng Y

    2013-01-01

    Yuangang Zu, Li Meng, Xiuhua Zhao, Yunlong Ge, Xinyang Yu, Yin Zhang, Yiping Deng Key Laboratory of Forest Plant Ecology, Northeast Forestry University, Ministry of Education, Harbin, People’s Republic of China Introduction: The livertaxis of glycyrrhizic acid-conjugated bovine serum albumin (GL-BSA) has been reported in the literature. Now, in this paper, we describe a novel type of drug-targeted delivery system containing 10-hydroxycamptothecin (HCPT) with liver tumor targeting. ...

  1. Synthesis of BSA/Fe3O4 magnetic composite microspheres for adsorption of antibiotics

    International Nuclear Information System (INIS)

    BSA/Fe3O4 magnetic composite microspheres with high saturation magnetization and paramagnetic property were prepared via inverse emulsion technology at room temperature, bovine serum albumin (BSA, 60 KD), magnetic nanoparticles (Fe3O4) and glutaraldehyde as macromonomer, inorganic particles and cross-linking agent, respectively. Fourier transform infrared (FTIR), scanning electron microscope (SEM), metalloscope, and particle size analyzer were used to characterize morphology and structure of composite microspheres. Vibrating sample magnetometer (VSM) and thermogravimetric analysis (TGA) were used to test magnetic properties of the synthesized samples, adsorption capacity of microspheres was determined by ultraviolet spectrophotometer (UV). The results showed that BSA/Fe3O4 microspheres were 43 μm with relatively narrow particle size distribution, perfect sphere-shaped morphologies, superparamagnetism with a saturation magnetization of 11 emu/g, and high magnetic content with a value of 57.29%. The main factors influencing properties of microspheres including raw material ratio, the amount of emulsifier and cross-linking agent, agitation speed were investigated and optimized. Furthermore, these microspheres accompanying with high separable and reusable efficient may have great potential application in the field of separation, in particular, removal of antibiotics. Adsorption capacities of the microspheres of four different kinds of antibiotics (erythromycin, streptomycin, tetracycline and chloramphenicol) ranging from 69.35 mg/g to 147.83 mg/g were obtained, and Langmuir isotherm model coincided with equilibrium data than that of the Freundlich model. - Highlights: • BSA/Fe3O4 microspheres with high saturation magnetization were prepared. • BSA/Fe3O4 microspheres for the removal of antibiotics are proposed. • The obtained results have significant importance in environmental processes

  2. Serum albumin 'camouflage' of plant virus based nanoparticles prevents their antibody recognition and enhances pharmacokinetics.

    Science.gov (United States)

    Pitek, Andrzej S; Jameson, Slater A; Veliz, Frank A; Shukla, Sourabh; Steinmetz, Nicole F

    2016-05-01

    Plant virus-based nanoparticles (VNPs) are a novel class of nanocarriers with unique potential for biomedical applications. VNPs have many advantageous properties such as ease of manufacture and high degree of quality control. Their biocompatibility and biodegradability make them an attractive alternative to synthetic nanoparticles (NPs). Nevertheless, as with synthetic NPs, to be successful in drug delivery or imaging, the carriers need to overcome several biological barriers including innate immune recognition. Plasma opsonization can tag (V)NPs for clearance by the mononuclear phagocyte system (MPS), resulting in shortened circulation half lives and non-specific sequestration in non-targeted organs. PEG coatings have been traditionally used to 'shield' nanocarriers from immune surveillance. However, due to broad use of PEG in cosmetics and other industries, the prevalence of anti-PEG antibodies has been reported, which may limit the utility of PEGylation in nanomedicine. Alternative strategies are needed to tailor the in vivo properties of (plant virus-based) nanocarriers. We demonstrate the use of serum albumin (SA) as a viable alternative. SA conjugation to tobacco mosaic virus (TMV)-based nanocarriers results in a 'camouflage' effect more effective than PEG coatings. SA-'camouflaged' TMV particles exhibit decreased antibody recognition, as well as enhanced pharmacokinetics in a Balb/C mouse model. Therefore, SA-coatings may provide an alternative and improved coating technique to yield (plant virus-based) NPs with improved in vivo properties enhancing drug delivery and molecular imaging. PMID:26950168

  3. Synthesis, capping and binding of colloidal gold nanoparticles to proteins

    International Nuclear Information System (INIS)

    Bovine serum albumin (BSA) was used as a stabilizing agent and biofunctionalized layer for water-dispersed gold nanoparticles (NPs) synthesized from metal precursor HAuCl4. The BSA binding to gold NPs was characterized qualitatively and quantitatively by transmission electron microscopy, UV-VIS and FTIR spectrophotometers. HER2 (human epidermal growth factor receptor 2) specific phage antibodies were attached to BSA stabilized gold NPs to form a gold–antibody complex. An ELISA (enzyme-linked immunosorbent assay) test was done to confirm the bioactivity of antibodies attached to gold NPs

  4. Effects of PEG size on structure, function and stability of PEGylated BSA

    DEFF Research Database (Denmark)

    Plesner, Bitten; Fee, Conan J.; Westh, Peter;

    2011-01-01

    The effects of PEGylation on the structural, thermal and functional stability of bovine serum albumin (BSA) were investigated using BSA and 6 linear mono-PEGylated BSA compounds. The secondary and tertiary structure of BSA measured by circular dichroism (CD) was independent of PEGylation. In...... unfolding temperature and the temperature of aggregation were both independent of the molecular weight of the PEG chain. Possible functional changes of BSA after PEGylation were measured by Isothermal Titration Calorimetry (ITC), where the binding of sodium dodecyl sulphate (SDS) to BSA and PEGylated BSA....... From the present biophysical characterisation, it is concluded that after PEGylation BSA appears to be unaffected structurally (secondary and tertiary structure), slightly destabilised thermally (unfolding temperature), stabilised kinetically (temperature of aggregation) and has an altered...

  5. A Gold Nanoparticle and Aflatoxin B1-BSA Conjugates Based Lateral Flow Assay Method for the Analysis of Aflatoxin B1

    Directory of Open Access Journals (Sweden)

    Sangdae Lee

    2012-04-01

    Full Text Available A rapid and simple immuno-chromatographic assay was developed to detect aflatoxin B1 (AFB1. The assay was based on a modified competitive binding format using colloidal gold and polyclonal antibody (Pab conjugates. The anti-AFB1 Pab was immobilized to a defined detection zone on a porous nitrocellulose membrane and colloidal gold particles were conjugated to AFB1-BSA which served as a detection reagent. The AFB1-containing sample was added to the membrane and allowed to move with AFB1-BSA-coated particles dried on the conjugation pad. The mixture was then passed along the porous membrane by capillary action past the Pab in the detection zone, which captured AFB1 or AFB1-BSA. AFB1 in the sample inhibits binding of AFB1-BSA conjugated gold particles to the Pab and prevents formation of a red color dot. In the absence of AFB1, AFB1-BSA conjugated gold particles bound to the Pab, give a red color within this detection zone. With this method, 10 μg/mL of AFB1 was detected in less than 10 min. The developed AFB1 assay also showed no cross reaction to Ochratoxin A (OTA.

  6. Interaction study on bovine serum albumin physically binding to silver nanoparticles: Evolution from discrete conjugates to protein coronas

    Science.gov (United States)

    Guo, Jun; Zhong, Ruibo; Li, Wanrong; Liu, Yushuang; Bai, Zhijun; Yin, Jun; Liu, Jingran; Gong, Pei; Zhao, Xinmin; Zhang, Feng

    2015-12-01

    The nanostructures formed by inorganic nanoparticles together with organic molecules especially biomolecules have attracted increasing attention from both industries and researching fields due to their unique hybrid properties. In this paper, we systemically studied the interactions between amphiphilic polymer coated silver nanoparticles and bovine serum albumins by employing the fluorescence quenching approach in combination with the Stern-Volmer and Hill equations. The binding affinity was determined to 1.30 × 107 M-1 and the interaction was spontaneously driven by mainly the van der Waals force and hydrogen-bond mediated interactions, and negatively cooperative from the point of view of thermodynamics. With the non-uniform coating of amphiphilic polymer, the silver nanoparticles can form protein coronas which can become discrete protein-nanoparticle conjugates when controlling their molar ratios of mixing. The protein's conformational changes upon binding nanoparticles was also studied by using the three-dimensional fluorescence spectroscopy.

  7. Tangential Flow Ultrafiltration Allows Purification and Concentration of Lauric Acid-/Albumin-Coated Particles for Improved Magnetic Treatment

    Directory of Open Access Journals (Sweden)

    Jan Zaloga

    2015-08-01

    Full Text Available Superparamagnetic iron oxide nanoparticles (SPIONs are frequently used for drug targeting, hyperthermia and other biomedical purposes. Recently, we have reported the synthesis of lauric acid-/albumin-coated iron oxide nanoparticles SEONLA-BSA, which were synthesized using excess albumin. For optimization of magnetic treatment applications, SPION suspensions need to be purified of excess surfactant and concentrated. Conventional methods for the purification and concentration of such ferrofluids often involve high shear stress and low purification rates for macromolecules, like albumin. In this work, removal of albumin by low shear stress tangential ultrafiltration and its influence on SEONLA-BSA particles was studied. Hydrodynamic size, surface properties and, consequently, colloidal stability of the nanoparticles remained unchanged by filtration or concentration up to four-fold (v/v. Thereby, the saturation magnetization of the suspension can be increased from 446.5 A/m up to 1667.9 A/m. In vitro analysis revealed that cellular uptake of SEONLA-BSA changed only marginally. The specific absorption rate (SAR was not greatly affected by concentration. In contrast, the maximum temperature Tmax in magnetic hyperthermia is greatly enhanced from 44.4 °C up to 64.9 °C by the concentration of the particles up to 16.9 mg/mL total iron. Taken together, tangential ultrafiltration is feasible for purifying and concentrating complex hybrid coated SPION suspensions without negatively influencing specific particle characteristics. This enhances their potential for magnetic treatment.

  8. Preparation and in vitro characterization of gallic acid-loaded human serum albumin nanoparticles

    International Nuclear Information System (INIS)

    Gallic acid (GA), as an antioxidant and antiparkinson agent, was loaded onto cationic human serum albumin nanoparticles (HSA NPs). Polyethylenimine (PEI)-coated HSA (PEI-HSA) NPs were prepared using three different methods: (I) coating negatively charged HSA NPs with positively charged PEI through attractive electrostatic interactions, (II) coating HSA NPs with PEI via covalent amide bond formation using N-(3-dimethylaminopropyl)-N-ethylcarbodiimide hydrochloride, and (III) coating HSA NPs with PEI via covalent bonding using glutaraldehyde for linking amine groups of PEI and amine groups of albumin NPs. Method II was selected since it resulted in a higher shift in the zeta potential value (mV) and less zeta potential value deviation, and also less size polydispersity. GA was loaded by adsorption onto the surface of PEI-HSA NPs of two different sizes: 117 ± 2.9 nm (PEI-P1) and 180 ± 3.1 nm (PEI-P2) NPs. Both GA-entrapment and GA-loading efficiencies increased slightly with the increasing size of NPs, and were affected intensely by the mass ratio of GA to PEI-HSA NPs. Free radical scavenging of GA was quantified based on the 2,2-diphenyl-1-picrylhydrazyl method. The obtained results showed that GA remains active during the preparation of GA-loaded PEI-HSA NPs. The cytotoxicities of HSA, PEI-HSA, and GA-loaded PEI-HSA NPs on the PC-12 cells, as the neuroendocrine cell line, were measured. Our results indicate that positively charged PEI-HSA NPs are good candidates for efficient and safe delivery of GA to the brain

  9. Preparation and in vitro characterization of gallic acid-loaded human serum albumin nanoparticles

    Energy Technology Data Exchange (ETDEWEB)

    Mohammad-Beigi, Hossein; Shojaosadati, Seyed Abbas, E-mail: shoja-sa@modares.ac.ir [Tarbiat Modares University, Biotechnology Group, Faculty of Chemical Engineering (Iran, Islamic Republic of); Morshedi, Dina; Arpanaei, Ayyoob [National Institute of Genetic Engineering and Biotechnology, Department of Industrial and Environmental Biotechnology (Iran, Islamic Republic of); Marvian, Amir Tayaranian [Aarhus University, Department of Biomedicine (Denmark)

    2015-04-15

    Gallic acid (GA), as an antioxidant and antiparkinson agent, was loaded onto cationic human serum albumin nanoparticles (HSA NPs). Polyethylenimine (PEI)-coated HSA (PEI-HSA) NPs were prepared using three different methods: (I) coating negatively charged HSA NPs with positively charged PEI through attractive electrostatic interactions, (II) coating HSA NPs with PEI via covalent amide bond formation using N-(3-dimethylaminopropyl)-N-ethylcarbodiimide hydrochloride, and (III) coating HSA NPs with PEI via covalent bonding using glutaraldehyde for linking amine groups of PEI and amine groups of albumin NPs. Method II was selected since it resulted in a higher shift in the zeta potential value (mV) and less zeta potential value deviation, and also less size polydispersity. GA was loaded by adsorption onto the surface of PEI-HSA NPs of two different sizes: 117 ± 2.9 nm (PEI-P1) and 180 ± 3.1 nm (PEI-P2) NPs. Both GA-entrapment and GA-loading efficiencies increased slightly with the increasing size of NPs, and were affected intensely by the mass ratio of GA to PEI-HSA NPs. Free radical scavenging of GA was quantified based on the 2,2-diphenyl-1-picrylhydrazyl method. The obtained results showed that GA remains active during the preparation of GA-loaded PEI-HSA NPs. The cytotoxicities of HSA, PEI-HSA, and GA-loaded PEI-HSA NPs on the PC-12 cells, as the neuroendocrine cell line, were measured. Our results indicate that positively charged PEI-HSA NPs are good candidates for efficient and safe delivery of GA to the brain.

  10. The Photochemical Study of HSA and BSA with Resonance Light-Scattering and Fluorescence Spectra

    Institute of Scientific and Technical Information of China (English)

    2000-01-01

    The resonance light-scattering (RLS) of human serum albumin (HSA) and bovine serum albumin (BSA) is reported for the first time, and applied to study photochemical reaction of HSA and BSA. The fact of photocrosslinking self-association effect in HSA and BSA solutions is identified by the enhancement of RLS. The fluorescence quenching at about 350 nm and 700 nm proves that tryptophan (Trp) residues are one of the photochemical activity sites in HSA and BSA molecules. The Rayleigh scattering (RS) spectra of HSA and BSA that were neglected in fluorescence spectra before are found at about 296 nm, 592 nm and 888 nm for the first time, and are of adventageous to studying the aggregation of HSA or BSA. The possible photochemical reaction mechanism is also proposed.

  11. Magnetic hydrogel beads based on PVA/sodium alginate/laponite RD and studying their BSA adsorption.

    Science.gov (United States)

    Mahdavinia, Gholam Reza; Mousanezhad, Sedigheh; Hosseinzadeh, Hamed; Darvishi, Farshad; Sabzi, Mohammad

    2016-08-20

    In this study double physically crosslinked magnetic hydrogel beads were developed by a simple method including solution mixing of sodium alginate and poly(vinyl alcohol) (PVA) containing magnetic laponite RD (Rapid Dispersion). Sodium alginate and PVA were physically crosslinked by Ca(2+) and freezing-thawing cycles, respectively. Magnetic laponite RD nanoparticles were incorporated into the system to create magnetic response and strengthen the hydrogels. All hybrids double physically crosslinked hydrogel beads were stable under different pH values without any disintegration. Furthermore, adsorption of bovine serum albumin (BSA) on the hydrogel beads was investigated on the subject of pH, ion strength, initial BSA concentration, and temperature. Nanocomposite beads exhibited maximum adsorption capacity for BSA at pH=4.5. The experimental adsorption isotherm data were well followed Langmuir model and based on this model the maximum adsorption capacity was obtained 127.3mgg(-1) at 308K. Thermodynamic parameters revealed spontaneous and monolayer adsorption of BSA on magnetic nanocomposites beads. PMID:27178944

  12. Effect of temperature on the methotrexate BSA interaction: Spectroscopic study

    Science.gov (United States)

    Sułkowska, A.; Maciążek, M.; Równicka, J.; Bojko, B.; Pentak, D.; Sułkowski, W. W.

    2007-05-01

    Rheumatoid arthritis (RA) is an autoimmune and chronic inflammatory illness which affects about one percent of the world's population. Methotrexate (4-amino-10-methylfolic acid) (MTX) also known as amethopterin is commonly used to treat rheumatoid arthritis (RA). It is transported in the circulary system as a complex with serum albumin. The aim of this study was to investigate the interactions of MTX with transporting protein with the use of spectroscopic methods. The binding of MTX to bovine serum albumin (BSA) was studied by monitoring the changes in the emission fluorescence spectra of protein in the presence of MTX at excitation wavelength of 280 nm and 295 nm. The quenching of protein fluorescence at temperature range from 298 K to 316 K was observed. Energy transfer between methotrexate and fluorophores contained in the serum albumin structure was found at the molar ratio MTX:BSA 7.5:1. The relative fluorescence intensity of BSA decreases with increase of temperature. Similar results were observed for BSA excited with 280 nm and 295 nm at the same temperature range. The presence of MTX seems to prevent these changes. Temperature dependence of the binding constant has been presented. The binding and quenching constants for equilibrium complex were calculated using Scatchard and Stern-Volmer method, respectively. The results show that MTX forms π-π complex with aromatic amino acid residues of BSA. The binding site for MTX on BSA was found to be situated in the hydrophobic IIA or IB subdomain where the Trps were located. The spontaneity of MTX-BSA complex formation in the temperature range 298-316 K was ascertained.

  13. Epitope imprinted polymer nanoparticles containing fluorescent quantum dots for specific recognition of human serum albumin

    International Nuclear Information System (INIS)

    Epitope imprinted polymer nanoparticles (EI-NPs) were prepared by one-pot polymerization of N-isopropylacrylamide in the presence of CdTe quantum dots and an epitope (consisting of amino acids 598 to 609) of human serum albumin (HSA). The resulting EI-NPs exhibit specific recognition ability and enable direct fluorescence quantification of HSA based on a fluorescence turn-on mode. The polymer was characterized by FT-IR, X-ray photoelectron spectroscopy, transmission electron microscopy and dynamic light scattering. The linear calibration graph was obtained in the range of 0.25–5 μmol · mL−1 with the detection limit of 44.3 nmol · mL−1. The EI-NPs were successfully applied to the direct fluorometric quantification of HSA in samples of human serum. Overall, this approach provides a promising tool to design functional fluorescent materials with protein recognition capability and specific applications in proteomics. (author)

  14. Water sorption and glass transition of amorphous sugars containing BSA

    Energy Technology Data Exchange (ETDEWEB)

    Imamura, K.; Suzuki, T.; Tatsumichi, T.; Kirii, S.; Okazaki, M. [Kyoto Univ., Kyoto (Japan). Dept. of Chemical Engineering

    2000-08-01

    Water sorption and glass transition of four amorphous sugars (lactose, maltose, sucrose, and trehalose) containing bovine serum albumin (BSA) are investigated. Freeze-dried sugar-BSA samples equilibrated at several water activities ranging from 0 to 0.43 were prepared. Moisture content and glass transition temperature (T{sub g}) were measured. For the all sugars, it is found that BSA lowers T{sub g} at low water activity, and raises it at high water activity. It is also found that the difference between T{sub g} of the sugar-BSA samples and that of the corresponding amorphous sugar samples (T{sub g0}) depends mainly on T{sub g0}. (author)

  15. Small angle X-ray scattering studies to access the influence of bovine serum albumin (BSA) and carbonic anhydrase (Boca) on the size and interaction among Aerosol-O T reversed micelles as a function of the micellar hydration degree

    International Nuclear Information System (INIS)

    Full text: Reversed micelles (RMs) of AOT (sodium bis-2-ethylhexyl sulfosuccinate) has constitute an efficient system to investigate membrane interaction and physical chemical behavior of short biologically active peptides, proteins and enzymes in water controlled environment and apolar medium. Information may be obtained from protein-membrane interaction, including solubilization, binding location, conformational changes, activity size droplet-dependent, and changes in the properties of RM environment, useful in studies in biocatalysis and bioseparation systems [1]. In this work, changes in the structural features and interactive forces among AOT RMs in hexane were monitored in several stages of micellar hydration W (= [buffer]/[0.1M AOT]), and in the presence of BSA (66.5 kDa) and BCA (30 Kda), by SAXS. The interactive forces between the RMs with proteins were analyzed within the framework of repulsion and attractive interaction potentials through the pairing stick hardsphere (PSHS) model [2]. In this way, the spherical core radius to the system of pure AOT RMs at W = 4, 10, 20 and 30 were respectively 15, 22, 33 and 43 A (20% of polydispersity), evaluated from the particle form factor P(q) modeling [1]. The PSHS analysis from SAXS curves of AOT RMs with BSA and BCA at smaller droplets size of 4 and 10, showed, respectively, an interplay between attractive and repulsive interactions between the micelles (attractive component in S(q) was predominant) with the preservation of the discrete RM radius in the presence of protein. On the other hand, for protein confined in the bigger RM droplet size with W=30, the attractive inter micellar forces were of minor importance for BSA and the appearing of a predominant repulsive hard sphere component in SAXS curves accompanied by a decreasing of the micellar radius to 36 A were detected. For BCA, however, at higher W (30), a phase separation was observed probably associated to the formation of unstable large BCA aggregates

  16. Use of biotin targeted methotrexate–human serum albumin conjugated nanoparticles to enhance methotrexate antitumor efficacy

    Directory of Open Access Journals (Sweden)

    Taheri A

    2011-09-01

    Full Text Available Azade Taheri1, Rassoul Dinarvand1,2, Faranak Salman Nouri1, Mohammad Reza Khorramizadeh3, Atefeh Taheri Borougeni4, Pooria Mansoori5, Fatemeh Atyabi1,21Department of Pharmaceutics, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran; 2Nanotechnology Research Centre, Faculty of Pharmacy, Tehran University of Medical sciences, Tehran, Iran; 3Department of Pathobiology, School of Public Health, Tehran University of Medical Sciences, Tehran, Iran; 4Department of Oral and Maxillofacial Pathology, Faculty of Dentistry, Tehran University of Medical Sciences, Tehran, Iran; 5Faculty of Medicine, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, IranAbstract: Biotin molecules could be used as suitable targeting moieties in targeted drug delivery systems against tumors. To develop a biotin targeted drug delivery system, we employed human serum albumin (HSA as a carrier. Methotrexate (MTX molecules were conjugated to HSA. MTX-HSA nanoparticles (MTX-HSA NPs were prepared from these conjugates by cross-linking the HSA molecules. Biotin molecules were then conjugated on the surface of MTX-HSA NPs. The anticancer efficacy of biotin targeted MTX-HSA NPs was evaluated in mice bearing 4T1 breast carcinoma. A single dose of biotin targeted MTX-HSA NPs showed stronger in vivo antitumor activity than non-targeted MTX-HSA NPs and free MTX. By 7 days after treatment, average tumor volume in the biotin targeted MTX-HSA NPs-treated group decreased to 17.6% of the initial tumor volume when the number of attached biotin molecules on MTX-HSA-NPs was the highest. Average tumor volume in non-targeted MTX-HSA NPs-treated mice grew rapidly and reached 250.7% of the initial tumor volume. Biotin targeted MTX-HSA NPs increased the survival of tumor-bearing mice to 47.5 ± 0.71 days and increased their life span up to 216.7%. Mice treated with biotin targeted MTX-HSA NPs showed slight body weight loss (8% 21 days after treatment, whereas non-targeted MTX

  17. Synthesis, purification and mass spectrometric characterisation of a fluorescent Au9@BSA nanocluster and its enzymatic digestion by trypsin

    Science.gov (United States)

    Fernández-Iglesias, Nerea; Bettmer, Jörg

    2013-12-01

    Nanoclusters of noble metals like Ag and Au have attracted great attention as they form a missing link between isolated metal atoms and nanoparticles. Their particular properties like luminescence in the visible range and nontoxicity make them attractive for bioimaging and biolabelling purposes, especially with use of proteins as stabilising agents. In this context, this study intends the synthesis of a specific Au nanocluster covered by bovine serum albumin (BSA). It is shown that size-exclusion chromatography is feasible for the purification and isolation of the nanocluster. A mass spectrometric characterisation, preferably by ESI-MS, indicates the presence of an Au9@BSA nanocluster. Enzymatic digestion of the nanocluster with trypsin results in a significant increase of the fluorescence intensity at 650 and 710 nm, whereas complementary MALDI-MS studies are presented for the identification of generated peptides and show a distinctive pattern in comparison to the pure protein. It can be concluded that Au9@BSA might be, in future, an interesting candidate for in vitro studies of protease activities.Nanoclusters of noble metals like Ag and Au have attracted great attention as they form a missing link between isolated metal atoms and nanoparticles. Their particular properties like luminescence in the visible range and nontoxicity make them attractive for bioimaging and biolabelling purposes, especially with use of proteins as stabilising agents. In this context, this study intends the synthesis of a specific Au nanocluster covered by bovine serum albumin (BSA). It is shown that size-exclusion chromatography is feasible for the purification and isolation of the nanocluster. A mass spectrometric characterisation, preferably by ESI-MS, indicates the presence of an Au9@BSA nanocluster. Enzymatic digestion of the nanocluster with trypsin results in a significant increase of the fluorescence intensity at 650 and 710 nm, whereas complementary MALDI-MS studies are presented

  18. BSA 310 UOP Course Tutorial / tutorialoutlet

    OpenAIRE

    Mary Balogh

    2015-01-01

    For more course tutorials visit www.tutorialoutlet.com BSA 310 Week 1 Discussion Question 1 (Uop) BSA 310 Week 1 Discussion Question 2 (Uop) BSA 310Week 2 Discussion Question 1 (Uop) BSA 310 Week 2 Discussion Question 2 (Uop) BSA 310 week 2 Individual Assignment Critical Information Systems Paper (Uop) BSA 310 Week 3 Discussion Question 1 (Uop) BSA 310 Week 3 Discussion Question 2 (Uop) BSA 310 week 3 Individual Assignment Service Request SR-kf-013 (Uop)  

  19. BSA 500 New Course Tutorial / tutorialoutlet

    OpenAIRE

    Mary Balogh

    2015-01-01

    For more course tutorials visit www.tutorialoutlet.com   BSA 500 Week Riordan Manufacturing Paper BSA 500 Week Calculate Financial Ratios BSA 500 Week Balance Sheet and Income Statement Commentary BSA 500 Week Virtual Organizations Table, Part II BSA 500 Week Virtual Organizations Table, Part  BSA 500 Week 6 Assignment Riordan Manufacturing 

  20. Protein nanoparticle interaction: A spectrophotometric approach for adsorption kinetics and binding studies

    Science.gov (United States)

    Vaishanav, Sandeep K.; Chandraker, Kumudini; Korram, Jyoti; Nagwanshi, Rekha; Ghosh, Kallol K.; Satnami, Manmohan L.

    2016-08-01

    Investigating the protein nanoparticle interaction is crucial to understand how to control the biological interactions of nanoparticles. In this work, Model protein Bovine serum albumin (BSA) was used to evaluate the process of protein adsorption to the gold nanoparticles (GNPs) surface. The binding of a model protein (BSA) to GNPs was investigated through fluorescence quenching measurements. The strong affinities of BSA for GNPs were confirmed by the high value of binding constant (Ks) which was calculated to be 2.2 × 1011 L/mol. In this consequence, we also investigated the adsorption behavior of BSA on GNPs surface via UV-Vis spectroscopy. The effect of various operational parameters such as pH, contact time, initial BSA concentration, and temperature on adsorption of BSA was investigated using batch adsorption experiments. Kinetics of adsorption was found to follow the pseudo-second order rate equation. The suitability of Freundlich and Langmuir adsorption models to the equilibrium data was investigated. The equilibrium adsorption was well described by the Freundlich isotherm model. The maximum adsorption capacity for BSA adsorbed on GNPs was 58.71 mg/g and equilibrium constant was 0.0058 calculated by the Langmuir model at 298 K and pH = 11.0. Thermodynamic parameters showed that the adsorption of BSA onto GNPs was feasible, spontaneous, and exothermic.

  1. Inhalable self-assembled albumin nanoparticles for treating drug-resistant lung cancer.

    Science.gov (United States)

    Choi, Seong Ho; Byeon, Hyeong Jun; Choi, Ji Su; Thao, Lequang; Kim, Insoo; Lee, Eun Seong; Shin, Beom Soo; Lee, Kang Choon; Youn, Yu Seok

    2015-01-10

    Direct pulmonary delivery of anti-cancer agents is viewed as an effective way of treating lung cancer. Here, we fabricated inhalable nanoparticles made of human serum albumin (HSA) conjugated with doxorubicin and octyl aldehyde and adsorbed with apoptotic TRAIL protein (TRAIL/Dox HSA-NP). The octyl aldehyde and doxorubicin endowed HSA with significant hydrophobicity that facilitated self-assembly. TRAIL/Dox HSA-NP was found to have excellent particle size (~340nm), morphology, dispersability, and aerosolization properties. TRAIL/Dox HSA-NP displayed synergistic cytotoxicity and apoptotic activity in H226 lung cancer cells vs. HSA-NP containing TRAIL or Dox alone. TRAIL/Dox HSA-NP was well deposited in the mouse lungs using an aerosolizer, and TRAIL and Dox-HSA were found to be gradually released over 3days. The anti-tumor efficacy of pulmonary administered TRAIL/Dox HSA-NP was evaluated in BALB/c nu/nu mice bearing H226 cell-induced metastatic tumors. It was found that the tumors of H226-implanted mice treated with TRAIL/Dox HSA-NP were remarkably smaller and lighter than those of mice treated with TRAIL or Dox HSA-NP alone (337.5±7.5; 678.2±51.5; and 598.9±24.8mg, respectively). Importantly, this improved anti-tumor efficacy was found to be due to the synergistic apoptotic effects of Dox and TRAIL. In the authors' opinion, TRAIL/Dox HSA-NP offers a potential inhalable anti-lung cancer drug delivery system. Furthermore, the synergism displayed by combined use of Dox and TRAIL could be used to markedly reduce doxorubicin doses and minimize its side effects. PMID:25445703

  2. Human Serum Albumin Nanoparticles for Use in Cancer Drug Delivery: Process Optimization and In Vitro Characterization

    Directory of Open Access Journals (Sweden)

    Nikita Lomis

    2016-06-01

    Full Text Available Human serum albumin nanoparticles (HSA-NPs are widely-used drug delivery systems with applications in various diseases, like cancer. For intravenous administration of HSA-NPs, the particle size, surface charge, drug loading and in vitro release kinetics are important parameters for consideration. This study focuses on the development of stable HSA-NPs containing the anti-cancer drug paclitaxel (PTX via the emulsion-solvent evaporation method using a high-pressure homogenizer. The key parameters for the preparation of PTX-HSA-NPs are: the starting concentrations of HSA, PTX and the organic solvent, including the homogenization pressure and its number cycles, were optimized. Results indicate a size of 143.4 ± 0.7 nm and 170.2 ± 1.4 nm with a surface charge of −5.6 ± 0.8 mV and −17.4 ± 0.5 mV for HSA-NPs and PTX-HSA-NPs (0.5 mg/mL of PTX, respectively. The yield of the PTX-HSA-NPs was ~93% with an encapsulation efficiency of ~82%. To investigate the safety and effectiveness of the PTX-HSA-NPs, an in vitro drug release and cytotoxicity assay was performed on human breast cancer cell line (MCF-7. The PTX-HSA-NPs showed dose-dependent toxicity on cells of 52%, 39.3% and 22.6% with increasing concentrations of PTX at 8, 20.2 and 31.4 μg/mL, respectively. In summary, all parameters involved in HSA-NPs’ preparation, its anticancer efficacy and scale-up are outlined in this research article.

  3. Dual chitosan/albumin-coated alginate/dextran sulfate nanoparticles for enhanced oral delivery of insulin.

    Science.gov (United States)

    Lopes, Marlene; Shrestha, Neha; Correia, Alexandra; Shahbazi, Mohammad-Ali; Sarmento, Bruno; Hirvonen, Jouni; Veiga, Francisco; Seiça, Raquel; Ribeiro, António; Santos, Hélder A

    2016-06-28

    The potential of nanoparticles (NPs) to overcome the barriers for oral delivery of protein drugs have led to the development of platforms capable of improving their bioavailability. However, despite the progresses in drug delivery technologies, the success of oral delivery of insulin remains elusive and the disclosure of insulin mechanisms of absorption remains to be clarified. To overcome multiple barriers faced by oral insulin and to enhance the insulin permeability across the intestinal epithelium, here insulin-loaded alginate/dextran sulfate (ADS)-NPs were formulated and dual-coated with chitosan (CS) and albumin (ALB). The nanosystem was characterized by its pH-sensitivity and mucoadhesivity, which enabled to prevent 70% of in vitro insulin release in simulated gastric conditions and allowed a sustained insulin release following the passage to simulated intestinal conditions. The pH and time-dependent morphology of the NPs was correlated to the release and permeation profile of insulin. Dual CS/ALB coating of the ADS-NPs demonstrated augmented intestinal interactions with the intestinal cells in comparison to the uncoated-NPs, resulting in a higher permeability of insulin across Caco-2/HT29-MTX/Raji B cell monolayers. The permeability of the insulin-loaded ALB-NPs was reduced after the temperature was decreased and after co-incubation with chlorpromazine, suggesting an active insulin transport by clathrin-mediated endocytosis. Moreover, the permeability inhibition with the pre-treatment with sodium chlorate suggested that the interaction between glycocalix and the NPs was critical for insulin permeation. Overall, the developed nanosystem has clinical potential for the oral delivery of insulin and therapy of type 1 diabetes mellitus. PMID:27074369

  4. Safety concerns towards the biomedical application of PbS nanoparticles: An approach through protein-PbS interaction and corona formation

    Energy Technology Data Exchange (ETDEWEB)

    Kumar Bhunia, Amit; Saha, Satyajit [Department of Physics and Technophysics, Vidyasagar University, Paschim Medinipur 721102 (India); Kanti Samanta, Pijus [Department of Physics, Ghatal R.S. Mahavidyalaya, Paschim Medinipur 721212 (India); Kamilya, Tapanendu, E-mail: tapanenduiacs@gmail.com [Department of Physics, Narajole Raj College, Paschim Medinipur 721211 (India)

    2014-03-24

    Semiconductor nanoparticles (NPs) with near-infrared (NIR) fluorescence has achieved great interest for early detection of colon tumors/cancer. We have synthesized lead sulphide (PbS) NPs (5–7 nm) having emission in NIR region and investigated its interaction with bovine serum albumin (BSA) to determine the bio-safety of PbS NPs. The interaction of PbS NPs with BSA occurs through formation of “hard” and “soft” protein NPs corona and follows exponential association. The hard corona represents that the core PbS NPs are fully covered by BSA with shell thickness of ∼8 nm, i.e., the dimension of BSA monomer. A large number of PbS NPs with hard corona of BSA forms “colony” with diameters in the range of 200–400 nm. The soft corona grows surrounding this colony. The quenching of fluorescence BSA in the presence of PbS NPs follows dynamic quenching process with tryptophan as major binding sites. Nearest to human body temperature, positive cooperative association between PbS NPs and BSA are found, and affinity of BSA to the PbS NPs gradually increases in superlinear fashion. The electrostatic interaction is the key force in binding of PbS NPs with BSA, and hydrophobic interaction between PbS NPs and BSA is responsible for conformational change of BSA.

  5. Biodegradable human serum albumin nanoparticles as contrast agents for the detection of hepatocellular carcinoma by magnetic resonance imaging.

    Science.gov (United States)

    Watcharin, Waralee; Schmithals, Christian; Pleli, Thomas; Köberle, Verena; Korkusuz, Hüdayi; Huebner, Frank; Zeuzem, Stefan; Korf, Hans W; Vogl, Thomas J; Rittmeyer, Claudia; Terfort, Andreas; Piiper, Albrecht; Gelperina, Svetlana; Kreuter, Jörg

    2014-05-01

    Tumor visualization by magnetic resonance imaging (MRI) and nanoparticle-based contrast agents may improve the imaging of solid tumors such as hepatocellular carcinoma (HCC). In particular, human serum albumin (HSA) nanoparticles appear to be a suitable carrier due to their safety and feasibility of functionalization. In the present study HSA nanoparticles were conjugated with gadolinium diethylenetriaminepentaacetic acid (Gd-DTPA) using carbodiimide chemistry. The nanoparticles had a uniform spherical shape and a diameter of 235±19nm. For better optical visualization in vitro and in vivo, the HSA-Gd nanoparticles were additionally labeled with rhodamine 123. As shown by confocal microscopy and flow cytometry analysis, the fluorescent nanoparticles were readily taken up by Huh-7 hepatocellular carcinoma cells. After 24h incubation in blood serum, less than 5% of the Gd(III) was released from the particles, which suggests that this nanoparticulate system may be stable in vivo and, therefore, may serve as potentially safe T1 MRI contrast agent for MRI of hepatocellular carcinoma. PMID:24365328

  6. Synthesis of BSA/Fe{sub 3}O{sub 4} magnetic composite microspheres for adsorption of antibiotics

    Energy Technology Data Exchange (ETDEWEB)

    Zhang, Baoliang; Zhang, Hepeng; Li, Xiangjie; Lei, Xingfeng; Li, Chunmei; Yin, Dezhong; Fan, Xinlong; Zhang, Qiuyu, E-mail: qyzhang@nwpu.edu.cn

    2013-10-01

    BSA/Fe{sub 3}O{sub 4} magnetic composite microspheres with high saturation magnetization and paramagnetic property were prepared via inverse emulsion technology at room temperature, bovine serum albumin (BSA, 60 KD), magnetic nanoparticles (Fe{sub 3}O{sub 4}) and glutaraldehyde as macromonomer, inorganic particles and cross-linking agent, respectively. Fourier transform infrared (FTIR), scanning electron microscope (SEM), metalloscope, and particle size analyzer were used to characterize morphology and structure of composite microspheres. Vibrating sample magnetometer (VSM) and thermogravimetric analysis (TGA) were used to test magnetic properties of the synthesized samples, adsorption capacity of microspheres was determined by ultraviolet spectrophotometer (UV). The results showed that BSA/Fe{sub 3}O{sub 4} microspheres were 43 μm with relatively narrow particle size distribution, perfect sphere-shaped morphologies, superparamagnetism with a saturation magnetization of 11 emu/g, and high magnetic content with a value of 57.29%. The main factors influencing properties of microspheres including raw material ratio, the amount of emulsifier and cross-linking agent, agitation speed were investigated and optimized. Furthermore, these microspheres accompanying with high separable and reusable efficient may have great potential application in the field of separation, in particular, removal of antibiotics. Adsorption capacities of the microspheres of four different kinds of antibiotics (erythromycin, streptomycin, tetracycline and chloramphenicol) ranging from 69.35 mg/g to 147.83 mg/g were obtained, and Langmuir isotherm model coincided with equilibrium data than that of the Freundlich model. - Highlights: • BSA/Fe{sub 3}O{sub 4} microspheres with high saturation magnetization were prepared. • BSA/Fe{sub 3}O{sub 4} microspheres for the removal of antibiotics are proposed. • The obtained results have significant importance in environmental processes.

  7. Water-soluble chitosan nanoparticles as a novel carrier system for protein delivery

    Institute of Scientific and Technical Information of China (English)

    WANG Chun; FU Xiong; YANG LianSheng

    2007-01-01

    High MW chitosan (CS) solutions have already been proposed as vehicles for protein delivery. The aim of the present work is to investigate the potential utility of water-soluble chitosan (WSC) as vehicles to load and deliver proteins. WSC nanoparticles (WSC NP) with various formations were prepared based on ionic gelation of WSC with pentasodium tripolyphosphate (TPP) anions. Bovine serum albumin (BSA) was used as a model protein drug incorporated into the WSC nanoparticles. Blank and BSA-loaded WSC nanoparticles were examined and determined to have a spherical shape with diameters between 35-190 nm, and zeta potential between 35-42 mV. FTIF confirmed that the tripolyphosphoric groups of TPP linked to the ammonium groups of WSC in the nanoparticles. Some factors affecting delivery properties of BSA have been investigated. Altering the concentration of BSA from 0.05 to 1 mg/mL enhanced the loading capacity of BSA but decreased loading efficiency simultaneously.Also, with the introduction of poly ethylene glycol (PEG), BSA release accelerated. Nanoparticle preparation from WSC with various deacetylation degrees (DDs) from 72.6% to 90% and MWs ranging from 3.5 to 15.8 kDa promoted loading efficiency and decreased the release rate. These results indicate that WSC nanoparticles are promising carriers for protein delivery.

  8. Evaluating interaction forces between BSA and rabbit anti-BSA in sulphathiazole sodium, tylosin and levofloxacin solution by AFM

    Science.gov (United States)

    Wang, Congzhou; Wang, Jianhua; Deng, Linhong

    2011-11-01

    Protein-protein interactions play crucial roles in numerous biological processes. However, it is still challenging to evaluate the protein-protein interactions, such as antigen and antibody, in the presence of drug molecules in physiological liquid. In this study, the interaction between bovine serum albumin (BSA) and rabbit anti-BSA was investigated using atomic force microscopy (AFM) in the presence of various antimicrobial drugs (sulphathiazole sodium, tylosin and levofloxacin) under physiological condition. The results show that increasing the concentration of tylosin decreased the single-molecule-specific force between BSA and rabbit anti-BSA. As for sulphathiazole sodium, it dramatically decreased the specific force at a certain critical concentration, but increased the nonspecific force as its concentration increasing. In addition, the presence of levofloxacin did not greatly influence either the specific or nonspecific force. Collectively, these results suggest that these three drugs may adopt different mechanisms to affect the interaction force between BSA and rabbit anti-BSA. These findings may enhance our understanding of antigen/antibody binding processes in the presence of drug molecules, and hence indicate that AFM could be helpful in the design and screening of drugs-modulating protein-protein interaction processes.

  9. Production of BSA-loaded alginate microcapsules: influence of spray dryer parameters on the microcapsule characteristics and BSA release.

    Science.gov (United States)

    Benchabane, Samir; Subirade, Muriel; Vandenberg, Grant W

    2007-09-01

    The aim of this study was to optimize the production of BSA-loaded alginate microcapsules by spray drying and to study the release of bovine serum albumin fraction V (BSA) under gastric simulated conditions. Microcapsule yield, BSA release, microcapsule size and size distribution were characterized following the application of different production parameters including inlet air temperature, inlet air pressure and liquid feed rate. The microcapsules were incubated in 0.1 N HCl and BSA release was quantified over time. The yields were higher with the pressure of 3 bar compared to 4 bar and with a feed rate of 0.45 vs. 0.2 ml s(-1). A high feed rate (0.45 vs. 0.2 ml s(-1)) allows one to obtain microcapsules with a low BSA release (p = 0.0327). The increase of the atomizer inlet temperature leads to microcapsules with a higher BSA release (p = 0.0230). A higher air pressure of 4 bar compared to 3 bar resulted in a lower microcapsule size (2.55 vs. 2.80 microm) and led to a narrower size distribution (0.92 vs. 1.07). In conclusion, the spray dryer parameters influenced the alginate microcapsule characteristics as well as subsequent protein release into a simulated gastric medium. PMID:17654176

  10. Logically Sensing Aggregate Process and Discriminating SDS from Other Surfactants with the Assistance of BSA

    Institute of Scientific and Technical Information of China (English)

    钱俊红; 徐玉芳; 钱旭红

    2012-01-01

    An amphiphilic fluorescent probe, 3-dodecylamino dihydrogen imidazo[2,l-a]benz[de]isoquinolin-7-one (compound 3), was used to sense the aggregate formation process of bovine serum albumine (BSA), sodium dode- cyl sulfate (SDS) and their mixed system. The fluorescence intensity of 3 was significantly affected by the adding order of SDS and BSA, and SDS can be distinguished from other surfactants with the aid of BSA, but only when 3 is allowed to interact with BSA first. The results revealed that compound 3 is preferentially sited in the hydrophobic region of BSA, and thermodynamically in SDS-BSA mixed aggregate. Sodium phosphate buffer solution (PBS) and BSA played important but distinct roles in distinguishing SDS micelle from the others.

  11. BSA 400 UOP Course Tutorial / tutorialoutlet

    OpenAIRE

    Mary Balogh

    2015-01-01

    For more course tutorials visit www.tutorialoutlet.com   BSA 400 Week 1 Individual Assignment Business Proposal and Project (UOP) BSA 400 Week 1 DQ 1 (UOP) BSA 400 Week 1 DQ 2 (UOP) BSA 400 Week 2 Individual Assignment Assessment of Enterprise Level Business Systems Paper (UOP) BSA 400 Week 2 DQ 1 (UOP)

  12. Prussian blue/serum albumin/indocyanine green as a multifunctional nanotheranostic agent for bimodal imaging guided laser mediated combinatorial phototherapy.

    Science.gov (United States)

    Sahu, Abhishek; Lee, Jong Hyun; Lee, Hye Gyeong; Jeong, Yong Yeon; Tae, Giyoong

    2016-08-28

    Developing novel nanotheranostic agent using only clinically approved materials is highly desirable and challenging. In this study, we combined three clinically approved materials, Prussian blue (PB), serum albumin (BSA), and indocyanine green (ICG), by a simple and biocompatible method to prepare a multifunctional theranostic PB-BSA-ICG nanoparticle. The multifunctional nanoparticle system could provide dual mode magnetic resonance (MR) and near infrared (NIR) fluorescence imaging as well as combined photothermal and photodynamic (PTT-PDT) therapy in response to a single NIR laser. This nanoparticle showed an excellent stability in physiological solutions and could suppress the photo-instability of ICG. In the absence of light, the nanoparticles showed no cytotoxicity, but significant cell death was induced through combined PTT-PDT effect after irradiation with NIR laser light. A high tumor accumulation and minimal nonspecific uptake by other major organs of PB-BSA-ICG nanoparticle were observed in vivo, analyzed by T1-weighted MR and NIR fluorescence bimodal imaging in tumor xenograft mice after intravenous injection. The nanoparticles efficiently suppressed the tumor growth through combinatorial phototherapy with no tumor recurrence upon a single NIR laser irradiation. These results demonstrated that PB-BSA-ICG is potentially an interesting nanotheranostic agent for imaging guided cancer therapy by overcoming the limitations of each technology and enhancing the therapeutic efficiency as well as reducing side effects. PMID:27349352

  13. The role of colloid particles in the albumin-lanthanides interaction: The study of aggregation mechanisms.

    Science.gov (United States)

    Tikhonova, Tatiana N; Shirshin, Evgeny A; Romanchuk, Anna Yu; Fadeev, Victor V

    2016-10-01

    We studied the interaction between bovine serum albumin (BSA) and lanthanide ions in aqueous solution in the 4.0÷9.5pH range. A strong increase of the solution turbidity was observed at pH values exceeding 6, which corresponds to the formation of Ln(OH)3 nanoparticles, while no changes were observed near the isoelectric point of BSA (pH 4.7). The results of the dynamic light scattering and protein adsorption measurements clearly demonstrated that the observed turbidity enhancement was caused by albumin sorption on the surface of Ln(OH)3 and colloid particles bridging via adsorbed protein molecules. Upon pH increase from 4.5 to 6.5, albumin adsorption on lanthanide colloids was observed, while the following increase of pH from 6.5 to 9.5 led to protein desorption. The predominant role of the electrostatic interactions in the adsorption and desorption processes were revealed in the zeta-potential measurements. No reversibility was observed upon decreasing pH from 9.5 to 4.5 that was suggested to be due to the other interaction mechanisms present in the system. It was shown that while for all lanthanide ions the interaction mechanism with BSA was similar, its manifestation in the optical properties of the system was significantly different. This was interpreted as a consequence of the differences in lanthanides hydrolysis constants. PMID:27419645

  14. Thin films of xyloglucans for BSA adsorption

    Energy Technology Data Exchange (ETDEWEB)

    Jo, T.A. [Department of Biochemistry and Molecular Biology, Federal University of Parana, Curitiba, PR (Brazil); Laboratory of Biopolymers, Department of Chemistry, Federal University of Parana, Curitiba, PR (Brazil); Petri, D.F.S. [Institute of Chemistry, University of Sao Paulo, Sao Paulo, SP (Brazil); Valenga, F. [Department of Biochemistry and Molecular Biology, Federal University of Parana, Curitiba, PR (Brazil); Laboratory of Biopolymers, Department of Chemistry, Federal University of Parana, Curitiba, PR (Brazil); Lucyszyn, N. [Laboratory of Biopolymers, Department of Chemistry, Federal University of Parana, Curitiba, PR (Brazil); Sierakowski, M.-R. [Laboratory of Biopolymers, Department of Chemistry, Federal University of Parana, Curitiba, PR (Brazil)], E-mail: mariarita.sierakowski@ufpr.br

    2009-03-01

    In this work, XG extracted from Tamarindus indica (XGT) and Copaifera langsdorffii (XGC) seeds were deposited onto Si wafers as thin films. The characteristics of XGT and XGC adsorbed layers were compared with a commercial XG sample (TKP, Tamarind kernel powder) by ellipsometry and atomic force microscopy (AFM). Moreover, the adsorption of oxidized derivative of XGT (To60) onto amino-terminated Si wafers and the immobilization of bovine serum albumin (BSA) onto polysaccharides covered wafers, as a function of pH, were also investigated. The XG samples presented molar ratios Glc:Xyl:Gal of 2.4:2.1:1 (XGC); 2.8: 2.3: 1 (XGT) and 1.9:1.9:1 (TKP). The structure of XGT and XGC was determined by O-methy alditol acetate derivatization and showed similar features, but XGC confirmed the presence of more {alpha}-D-Xyl branches due to more {beta}-D-Gal ends. XGT deposited onto Si adsorbed as fibers and small entities uniformly distributed, as evidenced by AFM, while TPK and XGC formed larger aggregates. The thickness of To60 onto amino-terminated surface was similar to that determined for XGT onto Si wafers. A maximum in the adsorbed amount of BSA occurred close to its isoelectric point (5.5). These findings indicate that XGT and To60 are potential materials for the development of biomaterials and biotechnological devices.

  15. Depolymerization of insulin amyloid fibrils by albumin-modified magnetic fluid

    Science.gov (United States)

    Siposova, Katarina; Kubovcikova, Martina; Bednarikova, Zuzana; Koneracka, Martina; Zavisova, Vlasta; Antosova, Andrea; Kopcansky, Peter; Daxnerova, Zuzana; Gazova, Zuzana

    2012-02-01

    Pathogenesis of amyloid-related diseases is associated with the presence of protein amyloid deposits. Insulin amyloids have been reported in a patient with diabetes undergoing treatment by injection of insulin and causes problems in the production and storage of this drug and in application of insulin pumps. We have studied the interference of insulin amyloid fibrils with a series of 18 albumin magnetic fluids (MFBSAs) consisting of magnetite nanoparticles modified by different amounts of bovine serum albumin (w/w BSA/Fe3O4 from 0.005 up to 15). We have found that MFBSAs are able to destroy amyloid fibrils in vitro. The extent of fibril depolymerization was affected by nanoparticle physical-chemical properties (hydrodynamic diameter, zeta potential and isoelectric point) determined by the BSA amount present in MFBSAs. The most effective were MFBSAs with lower BSA/Fe3O4 ratios (from 0.005 to 0.1) characteristic of about 90% depolymerizing activity. For the most active magnetic fluids (ratios 0.01 and 0.02) the DC50 values were determined in the range of low concentrations, indicating their ability to interfere with insulin fibrils at stoichiometric concentrations. We assume that the present findings represent a starting point for the application of the active MFBSAs as therapeutic agents targeting insulin amyloidosis.

  16. Depolymerization of insulin amyloid fibrils by albumin-modified magnetic fluid

    International Nuclear Information System (INIS)

    Pathogenesis of amyloid-related diseases is associated with the presence of protein amyloid deposits. Insulin amyloids have been reported in a patient with diabetes undergoing treatment by injection of insulin and causes problems in the production and storage of this drug and in application of insulin pumps. We have studied the interference of insulin amyloid fibrils with a series of 18 albumin magnetic fluids (MFBSAs) consisting of magnetite nanoparticles modified by different amounts of bovine serum albumin (w/w BSA/Fe3O4 from 0.005 up to 15). We have found that MFBSAs are able to destroy amyloid fibrils in vitro. The extent of fibril depolymerization was affected by nanoparticle physical–chemical properties (hydrodynamic diameter, zeta potential and isoelectric point) determined by the BSA amount present in MFBSAs. The most effective were MFBSAs with lower BSA/Fe3O4 ratios (from 0.005 to 0.1) characteristic of about 90% depolymerizing activity. For the most active magnetic fluids (ratios 0.01 and 0.02) the DC50 values were determined in the range of low concentrations, indicating their ability to interfere with insulin fibrils at stoichiometric concentrations. We assume that the present findings represent a starting point for the application of the active MFBSAs as therapeutic agents targeting insulin amyloidosis. (paper)

  17. The novel preparation of 99mTc(I)-labeled human serum albumin (HSA) nanoparticles as a SPECT imaging agent

    International Nuclear Information System (INIS)

    The purpose of this study was to develop a convenient and robust method for preparation of 99mTc(I)-labeled human serum albumin nanoparticles (HSA-NPs) as a SPECT agent for tumor imaging. Efficient radiolabeling 99mTc to HSA-NPs was achieved by simply reacting [99mTc(OH2)3(CO)3]+ with the reconstituted HSA-NPs solution. The size and morphology of 99mTc(I)-HSA-NPs were analyzed and found not to significantly change after the preformed HSA-NPs were lyophilized or labeled with 99mTc(I). By incubating 99mTc(I)-HSA-NPs in rat plasma at 37 deg C for 30 h, 75 % of the radioactivity were found to be remained in the particles, suggesting good in vitro stability. (author)

  18. Quantifying the influence of polymer coatings on the serum albumin corona formation around silver and gold nanoparticles

    Energy Technology Data Exchange (ETDEWEB)

    Treuel, Lennart, E-mail: lennart.treuel@kit.edu [Karlsruhe Institute of Technology (KIT), Institute of Applied Physics and Center for Functional Nanostructures (CFN) (Germany); Malissek, Marcelina; Grass, Stefan [University of Duisburg-Essen, Institute for Physical Chemistry (Germany); Diendorf, Joerg; Mahl, Dirk; Meyer-Zaika, Wolfgang; Epple, Matthias [University of Duisburg-Essen, Institute of Inorganic Chemistry and Center for Nanointegration Duisburg-Essen (CeNIDE) (Germany)

    2012-09-15

    When nanoparticles (NPs) come into contact with biological fluids, proteins, and other biomolecules interact with their surface. Upon exposure to biological fluids a layer of proteins adsorbs onto their surface, the so-called protein corona, and interactions of biological systems with NPs are therefore mediated by this corona. Here, interactions of serum albumin with silver and gold NPs were quantitatively investigated using circular dichroism spectroscopy. Moreover, surface enhanced Raman spectroscopy was used for further elucidation of protein binding to silver surfaces. The decisive role of poly(vinylpyrrolidone), coatings on the protein adsorption was quantitatively described for the first time and the influential role of the polymer coatings is discussed. Research in nanotoxicology may benefit from such molecular scale data as well as scientific approaches seeking to improve nanomedical applications by using a wide range of polymer surface coatings to optimize biological transport and medical action of NPs.

  19. Improvement of the stability and activity of immobilized trypsin on modified Fe3O4 magnetic nanoparticles for hydrolysis of bovine serum albumin and its application in the bovine milk.

    Science.gov (United States)

    Atacan, Keziban; Çakıroğlu, Bekir; Özacar, Mahmut

    2016-12-01

    Trypsin (EC 3.4.21.4) was successfully immobilized on the surface of Fe3O4 magnetic nanoparticles that had been pre-treated with gallic acid (GA). Measurements of protein load by using Bradford assay and the trypsin-catalyzed hydrolysis of Nα-Benzoyl-dl-arginine 4-nitroanilide hydrochloride (BApNA) were made for the immobilized enzyme. By using magnetic nanoparticles, which provides easy separation and decent support material for enzyme immobilization with high surface area to volume ratio, and by employing biocompatible material gallic acid, immobilized enzyme system was synthesized along with improving trypsin activity and stability. Immobilized trypsin (TR) was more stable than the free one and demonstrated higher enzymatic activity at elevated temperatures (45-55°C) and in the alkaline pH region (6-10.5). Fe3O4 NPs-GA-TR retained 92% of its initial activity after 120days of storage at 4°C in sodium phosphate buffer (0.1M, pH 7.5), whereas the free trypsin maintained about 64% of its initial activity during the same storage period. In addition, activity of the immobilized trypsin was preserved 54.5% of its initial activity after eight times successive reuse. The Michaelis-Menten kinetic constant (Km) and maximum reaction velocity (Vmax) for free trypsin were 5.1mM and 23mM/min, respectively, whereas Km and Vmax values of immobilized trypsin were 7.88mM and 18.3mM/min, respectively. The performance of the immobilized trypsin was demonstrated by carrying out the hydrolysis of bovine serum albumin (BSA) within 1h, and the assay was performed by using liquid chromatography-mass spectrometry (LC-MS/MS) technique. The hydrolysis of bovine milk as a real food was investigated by immobilized trypsin using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). PMID:27374556

  20. Binding equilibrium study of phosphotungstic acid and HSA or BSA with UV spectrum, fluorescence spectrum and equilibrium dialysis

    Institute of Scientific and Technical Information of China (English)

    黄瑾; 袁余洲; 梁宏

    2002-01-01

    The binding equilibrium between phosphotungstic acid (H7[P(W2O7)6]@XH2O;PTA) and human serum albumin (HSA) or bovine serum albumin (BSA) has been studied by UV-Vis, fluorescence spectroscopies and equilibrium dialysis. It has been observed that UV absorption enhanced and the fluorescence quenched as the PTA binding to HSA or BSA at physiological pH 7.43( ± 0.02). The Scatchard analysis indicated that there exists a strong binding site of PTA in both HSA and BSA, and the successive stability constants of these two systems are obtained by nonlinear least-squares methods fitting Bjerrum formula.

  1. Combined image guided monitoring the pharmacokinetics of rapamycin loaded human serum albumin nanoparticles with a split luciferase reporter

    Science.gov (United States)

    Wang, Fu; Yang, Kai; Wang, Zhe; Ma, Ying; Gutkind, J. Silvio; Hida, Naoki; Niu, Gang; Tian, Jie

    2016-02-01

    Imaging guided techniques have been increasingly employed to investigate the pharmacokinetics (PK) and biodistribution of nanoparticle based drug delivery systems. In most cases, however, the PK profiles of drugs could vary significantly from those of drug delivery carriers upon administration in the blood circulation, which complicates the interpretation of image findings. Herein we applied a genetically encoded luciferase reporter in conjunction with near infrared (NIR) fluorophores to investigate the respective PK profiles of a drug and its carrier in a biodegradable drug delivery system. In this system, a prototype hydrophobic agent, rapamycin (Rapa), was encapsulated into human serum albumin (HSA) to form HSA Rapa nanoparticles, which were then labeled with Cy5 fluorophore to facilitate the fluorescence imaging of HSA carrier. Meanwhile, we employed transgenetic HN12 cells that were modified with a split luciferase reporter, whose bioluminescence function is regulated by Rapa, to reflect the PK profile of the encapsulated agent. It was interesting to discover that there existed an obvious inconsistency of PK behaviors between HSA carrier and rapamycin in vitro and in vivo through near infrared fluorescence imaging (NIFRI) and bioluminescence imaging (BLI) after treatment with Cy5 labeled HSA Rapa. Nevertheless, HSA Rapa nanoparticles manifested favorable in vivo PK and tumor suppression efficacy in a follow-up therapeutic study. The developed strategy of combining a molecular reporter and a fluorophore in this study could be extended to other drug delivery systems to provide profound insights for non-invasive real-time evaluation of PK profiles of drug-loaded nanoparticles in pre-clinical studies.Imaging guided techniques have been increasingly employed to investigate the pharmacokinetics (PK) and biodistribution of nanoparticle based drug delivery systems. In most cases, however, the PK profiles of drugs could vary significantly from those of drug delivery

  2. BSA 500 UOP Course Tutorial / tutorialoutlet

    OpenAIRE

    J. M. Barrie

    2015-01-01

    For more course tutorials visit www.tutorialoutlet.com   BSA 500 Week 1 Learning Team Charter (UOP) BSA 500 Week 2 Individual Assignment Virtual Organizations Table Part I (UOP) BSA 500 Week 3 Individual Assignment Table 1 Part 2 Virtual Organization (UOP) BSA 500 Week 4 Individual Assingment Balance Sheet and Income Statement (UOP)

  3. BSA 376 UOP Course Tutorial / tutorialoutlet

    OpenAIRE

    Mary Balogh

    2015-01-01

    For more course tutorials visit www.tutorialoutlet.com BSA 376 Week 2 Team Project Draft - Riordan Manufacturing Outline BSA 376 Week 3 Work Related Project Analysis Part 2 BSA 376 Week 3 Team Project Draft (Riordan Manufacturing) BSA 376 Week 5 SDLC Paper and Presentation

  4. Resonance energy transfer between fluorescent BSA protected Au nanoclusters and organic fluorophores

    Science.gov (United States)

    Raut, Sangram; Rich, Ryan; Fudala, Rafal; Butler, Susan; Kokate, Rutika; Gryczynski, Zygmunt; Luchowski, Rafal; Gryczynski, Ignacy

    2013-12-01

    Bovine serum albumin (BSA) protected nanoclusters (Au and Ag) represent a group of nanomaterials that holds great promise in biophysical applications due to their unique fluorescence properties and lack of toxicity. These metal nanoclusters have utility in a variety of disciplines including catalysis, biosensing, photonics, imaging and molecular electronics. However, they suffer from several disadvantages such as low fluorescence quantum efficiency (typically near 6%) and broad emission spectrum (540 nm to 800 nm). We describe an approach to enhance the apparent brightness of BSA Au clusters by linking them with a high extinction donor organic dye pacific blue (PB). In this conjugate PB acts as a donor to BSA Au clusters and enhances its brightness by resonance energy transfer (RET). We found that the emission of BSA Au clusters can be enhanced by a magnitude of two-fold by resonance energy transfer (RET) from the high extinction donor PB, and BSA Au clusters can act as an acceptor to nanosecond lifetime organic dyes. By pumping the BSA Au clusters using a high extinction donor, one can increase the effective brightness of less bright fluorophores like BSA Au clusters. Moreover, we prepared another conjugate of BSA Au clusters with the near infrared (NIR) dye Dylight 750 (Dy750), where BSA Au clusters act as a donor to Dy750. We observed that BSA Au clusters can function as a donor, showing 46% transfer efficiency to the NIR dye Dy750 with a long lifetime component in the acceptor decay through RET. Such RET-based probes can be used to prevent the problems of a broad emission spectrum associated with the BSA Au clusters. Moreover, transferring energy from BSA Au clusters to Dy750 will result in a RET probe with a narrow emission spectrum and long lifetime component which can be utilized in imaging applications.Bovine serum albumin (BSA) protected nanoclusters (Au and Ag) represent a group of nanomaterials that holds great promise in biophysical applications due to

  5. Choline-induced selective fluorescence quenching of acetylcholinesterase conjugated Au@BSA clusters.

    Science.gov (United States)

    Mathew, Meegle S; Baksi, Ananya; Pradeep, T; Joseph, Kuruvilla

    2016-07-15

    We have developed a highly selective sensitive fluorescent detection of acetylcholine (ACh) using bovine serum albumin (BSA) protected atomically precise clusters of gold. The gold quantum clusters (AuQC@BSA) synthesized using bovine serum albumin and conjugated with acetylcholinesterase (AChE), an enzyme specific for acetylcholine, resulting in AuQC@BSA-AChE. The enzyme, AChE hydrolyzes acetylcholine (ACh) to choline (Ch) which in turn interacts with AuQC@BSA-AChE and quenches its fluorescence, enabling sensing. We have carried out the real time monitoring of the hydrolysis of ACh using electrospray ionization mass spectrometry (ESI MS) to find out the mechanism of fluorescent quenching. The validity of present method for determination of concentration of acetylcholine in real system such as blood was demonstrated. Further, the sensor, AuQC@BSA-AChE can be easily coated on paper and an efficient and cheap sensor can be developed and detection limit for ACh is found to be 10nM. The fluorescent intensity of AuQC@BSA-AChE is sensitive towards acetylcholine in range of 10nM to 6.4µM. This suggests that AuQC@BSA-AChE has an excellent potential to be used for diagnosis of various neuropsychological and neuropsychiatric disorders. PMID:26921554

  6. Synthesis of 5-Fluorouracil conjugated LaF3:Tb3+/PEG-COOH nanoparticles and its studies on the interaction with bovine serum albumin: spectroscopic approach

    International Nuclear Information System (INIS)

    The luminescent lanthanide-doped nanoparticles have gathered considerable attention in many fields especially in biomedicine. In this work, the lanthanum fluoride-doped terbium nanoparticles (LaF3:Tb3+ NPs) via simple chemical precipitation method has been synthesized and functionalized with polyethylene glycol. The size and the shape of the nanoparticles are confirmed using X-ray diffraction and transmission electron microscopy. The conjugation of 5-Fluorouracil (5-FU) and thus synthesized nanoparticles (NPs) were confirmed using various spectroscopic methods such as UV–Visible spectroscopy, fluorescence steady state, and excited state spectroscopy studies. The enhancement in fluorescence emission (λ = 543 nm) of drug-conjugated nanoparticles confirms the Vander Waals force of attraction due to F–F bonding between the drug and the nanoparticles. Further, the effects of 5FU-NPs in carrier protein were investigated using bovine serum albumin as a protein model. The 5FU–LaF3:Tb3+ nanoparticles binding is illustrated with binding constant and number of binding sites. The structural change of bovine serum albumin has been studied using circular dichroism and Fourier transform infrared spectroscopy analysis.

  7. BSA 502 UOP Course Tutorial / tutorialoutlet

    OpenAIRE

    Paul Bailey

    2015-01-01

    For more course tutorials visit www.tutorialoutlet.com   BSA 502 Week 2 Individual Assignment Marketing Issues Paper (Kudler Fine Foods) (UOP) BSA 502 Week 2 Team Assignment Sales and Marketing Paper (Riordan Manufacturing) (UOP) BSA 502 Week 3 Individual Assignment Human Resource Paper (Kudler Fine Foods) (UOP) BSA 502 Week 3 Team Assignment Human Resources Paper ( Riordan Manufacturing) (UOP) BSA 502 Week 4 Individual Assignment Operations and Logistics Issu...

  8. Concurrent zero-dimensional and one-dimensional biomineralization of gold from a solution of Au3+ and bovine serum albumin

    International Nuclear Information System (INIS)

    A technique was developed for preparing a novel material that consists of gold nanoparticles trapped within a fiber of unfolded proteins. These fibers are made in an aqueous solution that contains HAuCl4 and the protein, bovine serum albumin (BSA). By changing the ratio of gold to BSA in solution, two different types of outcomes are observed. At lower gold to BSA ratios (30–120), a purple solution results after heating the mixture at 80 °C for 4 h. At higher gold to BSA ratios (130–170), a clear solution containing purple fibers results after heating the mixture at 80 °C for 4 h. UV–Vis spectroscopy and light scattering techniques show growth in nanocolloid size as gold to BSA ratio rises above 100. Data indicate that, for the higher gold to BSA ratios, the gold is sequestered within the solid material. The material mass, visible by eye, appears to be an aggregation of smaller individual fibers. Scanning electron microscopy and transmission electron microscopy indicate that these fibers are primarily one-dimensional aggregates, which can display some branching, and can be as narrow as 400 nm in size. The likely mechanism for the synthesis of the novel material is discussed. (paper)

  9. Physico-chemical and toxicological characterization of iron-containing albumin nanoparticles as platforms for medical imaging.

    Science.gov (United States)

    Rosenberger, Ina; Schmithals, Christian; Vandooren, Jennifer; Bianchessi, Silvia; Milani, Paolo; Locatelli, Erica; Israel, Liron L; Hübner, Frank; Matteoli, Michela; Lellouche, Jean-Paul; Franchini, Mauro Comes; Passoni, Lorena; Scanziani, Eugenio; Opdenakker, Ghislain; Piiper, Albrecht; Kreuter, Jörg

    2014-11-28

    Iron oxide-containing magnetic nanoparticles (MNPs) have certain advantages over currently used contrast agents for tumor imaging by magnetic resonance imaging (MRI) as they offer the possibility of functionalization with ligands and tracers. Functionalized MNPs also may be used for targeted tumor therapy. In the current study nanoparticles (NPs) consisting of recombinant human serum albumin (rHSA) with incorporated hydrophilic (NH4)2Ce(IV)(NO3)6-γ-Fe2O3 particles (CAN maghemite particles) for medical imaging were produced and characterized. For this purpose CAN maghemite particles were incorporated into an rHSA matrix to yield rHSA-NPs. The resulting NPs were analyzed by transmission electron microscopy, photon correlation spectroscopy, and atomic absorption. The sizes of the manufactured NP were 170 ± 10 nm, and the zeta-potential was -50 ± 3 mV. The NPs remained stable when stored after lyophilization with sucrose 3% [w/v] as a cryoprotector. They showed pro-inflammatory properties without cell and animal toxicity in vivo and were highly contrasting in MRI. In conclusion, this report introduces novel rHSA NP with favorable properties containing iron oxide for detection by MRI. PMID:25173842

  10. Human serum albumin nanoparticles as an efficient noscapine drug delivery system for potential use in breast cancer: preparation and in vitro analysis.

    Science.gov (United States)

    Sebak, Safaa; Mirzaei, Maryam; Malhotra, Meenakshi; Kulamarva, Arun; Prakash, Satya

    2010-01-01

    Drug delivery systems such as nanoparticles can provide enhanced efficacy for anticancer agents. Noscapine, a widely used cough suppressant for decades has recently been shown to cause significant inhibition and regression of tumor volumes without any detectable toxicity in cells or tissues. Nanoparticles made of human serum albumin (HSA) represent promising strategy for targeted drug delivery to tumor cells by enhancing the drug's bioavailability and distribution, and reducing the body's response towards drug resistance. In the present study, we report for the first time the incorporation and delivery of noscapine-loaded HSA nanoparticles to tumor cells. The nanoparticles were designed and optimized to achieve a particle size in the range of 150-300 nm with a drug-loading efficiency of 85%-96%. The nanoparticles were evaluated in vitro for their anticancer activity and efficacy on breast cancer cells. PMID:20957217

  11. Preparation and biodistribution of 188Re-labeled folate conjugated human serum albumin magnetic cisplatin nanoparticles (188Re-folate-CDDP/HSA MNPs in vivo

    Directory of Open Access Journals (Sweden)

    Tang QS

    2011-11-01

    Full Text Available Qiu-Sha Tang1,*, Dao-Zhen Chen2,*, Wen-Qun Xue2, Jing-Ying Xiang2, Yong-Chi Gong1, Li Zhang2, Cai-Qin Guo21Department of Pathology and Pathophysiology, Medical College, Southeast University, Nanjing, Jiangsu; 2Central Laboratory, Wuxi Hospital for Maternal and Child Health Care, Affiliated Medical School of Nanjin, Wuxi, Jiangsu, China *Authors contributed equally to this workBackground: The purpose of this study was to develop intraperitoneal hyperthermic therapy based on magnetic fluid hyperthermia, nanoparticle-wrapped cisplatin chemotherapy, and magnetic particles of albumin. In addition, to combine the multiple-killing effects of hyperthermal targeting therapy, chemotherapy, and radiotherapy, the albumin-nanoparticle surfaces were linked with radionuclide 188Re-labeled folic acid ligand (188Re-folate-CDDP/HSA.Methods: Human serum albumin was labeled with 188Re using the pre-tin method. Reaction time and optimal conditions of labeling were investigated. The particles were intravenously injected into mice, which were sacrificed at different time points. Radioactivity per gram of tissue of percent injected dose (% ID/g was measured in vital organs. The biodistribution of 188Re-folate-CDDP/HAS magnetic nanoparticles was assessed.Results: Optimal conditions for 188Re-labeled folate-conjugated albumin combined with cisplatin magnetic nanoparticles were: 0.1 mL of sodium gluconate solution (0.3 mol/L, 0.1 mL of concentrated hydrochloric acid with dissolved stannous chloride (10 mg/mL, 0.04 mL of acetic acid buffer solution (pH 5, 0.2 mol/L, 30 mg of folate-conjugated albumin combined with cisplatin magnetic nanoparticles, and 188ReO4 eluent (0.1 mL. The rate of 188Re-folate-CDDP-HSA magnetic nanoparticle formation exceeded 90%, and radiochemical purity exceeded 95%. The overall labeling rate was 83% in calf serum at 37°C. The major uptake tissues were the liver, kidney, intestine, and tumor after the 188Re-folate-CDDP/HSA magnetic nanoparticles

  12. Synthesis and conjugation of ZnO nanoparticles with bovine serum albumin for biological applications

    Science.gov (United States)

    Kumar, Pawan; Kumar, Parveen; Deep, Akash; Bharadwaj, Lalit M.

    2013-04-01

    Semiconductor nanomaterials tagged with biomarkers may be used for an early fluorescence-based detection of breast cancer. ZnO nanoparticles are water-soluble, non-toxic, photo-chemically stable with highly fluorescence applicability and are regarded for their possible biocompatibility. As a long-term research planning, we are aiming to use QDs conjugated with serum-biomarker for the diagnosis of breast cancer. The present work is a part in the said direction and reports preliminary observations on the synthesis and conjugation of ZnO nanoparticles with a representative protein marker.

  13. Competitive interactions between glucose and lactose with BSA: which sugar is better for children?

    Science.gov (United States)

    Zhang, Qiulan; Ni, Yongnian; Kokot, Serge

    2016-04-01

    The interactions of the sugars glucose and lactose with the transport protein bovine serum albumin (BSA) were investigated using fluorescence, FT-IR and circular dichroism (CD) techniques. The results indicated that glucose could be bonded and transported by BSA, mainly involving hydrogen bonds and van der Waals interactions (ΔH = -86.13 kJ mol(-1)). The obtained fluorescence data from the binding of sugar and BSA were processed by the multivariate curve resolution-alternating least squares (MCR-ALS) method, and the extracted concentration profiles showed that the equilibrium constant, rglucose:BSA, was about 7. However, the binding of lactose to BSA did not quench the fluorescence significantly, and this indicated that lactose could not be directly transported by BSA. The binding experiments were further performed using the fluorescence titration method in the presence of calcium and BSA. Calcium was added so that the calcium/BSA reactions could be studied in the presence or absence of glucose, lactose or hydrolysis products. The results showed that hydrolyzed lactose seemed to enhance calcium absorption in bovine animals. It would also appear that for children, lactose provides better nutrition; however, glucose is better for adults. PMID:26906109

  14. Spectroscopic studies on the interaction between phycocyanin and bovine serum albumin

    Science.gov (United States)

    Kathiravan, A.; Chandramohan, M.; Renganathan, R.; Sekar, S.

    2009-02-01

    Bluish phycocyanin was obtained from the cyanobacteria namely Spirulina sp. (marine form). The interaction between phycocyanin and bovine serum albumin (BSA) was studied by using absorption, FT-IR, steady-state, time resolved and synchronous fluorescence spectroscopy. Phycocyanin effectively quenched the intrinsic fluorescence of BSA. The number of binding sites ( n) and binding constant ( K) was measured by fluorescence quenching method. The interaction between phycocyanin and BSA occurs through static quenching and conformational changes of BSA were observed.

  15. Voltammetric Studies of the Interaction of Tris (1, 10-phenanthroline) Cobalt (Ⅲ) with Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    2001-01-01

    The voltammetric methods were used to prove the interaction of metal complex Co(phen)33+ with bovine serum albumin (BSA). The interaction of BSA with Co(phen)33+ molecules using BSA-modified electrode is described. Information of the binding ratio and interaction mode can be obtained from their electrochemical behavior and electrochemical data. Furthermore, attenuated total reflection infrared experiment was performed to prove the interaction between complexes and BSA.

  16. Albumin-coated SPIONs: an experimental and theoretical evaluation of protein conformation, binding affinity and competition with serum proteins

    Science.gov (United States)

    Yu, Siming; Perálvarez-Marín, Alex; Minelli, Caterina; Faraudo, Jordi; Roig, Anna; Laromaine, Anna

    2016-07-01

    The variety of nanoparticles (NPs) used in biological applications is increasing and the study of their interaction with biological media is becoming more important. Proteins are commonly the first biomolecules that NPs encounter when they interact with biological systems either in vitro or in vivo. Among NPs, super-paramagnetic iron oxide nanoparticles (SPIONs) show great promise for medicine. In this work, we study in detail the formation, composition, and structure of a monolayer of bovine serum albumin (BSA) on SPIONs. We determine, both by molecular simulations and experimentally, that ten molecules of BSA form a monolayer around the outside of the SPIONs and their binding strength to the SPIONs is about 3.5 × 10-4 M, ten times higher than the adsorption of fetal bovine serum (FBS) on the same SPIONs. We elucidate a strong electrostatic interaction between BSA and the SPIONs, although the secondary structure of the protein is not affected. We present data that supports the strong binding of the BSA monolayer on SPIONs and the properties of the BSA layer as a protein-resistant coating. We believe that a complete understanding of the behavior and morphology of BSA-SPIONs and how the protein interacts with SPIONs is crucial for improving NP surface design and expanding the potential applications of SPIONs in nanomedicine.The variety of nanoparticles (NPs) used in biological applications is increasing and the study of their interaction with biological media is becoming more important. Proteins are commonly the first biomolecules that NPs encounter when they interact with biological systems either in vitro or in vivo. Among NPs, super-paramagnetic iron oxide nanoparticles (SPIONs) show great promise for medicine. In this work, we study in detail the formation, composition, and structure of a monolayer of bovine serum albumin (BSA) on SPIONs. We determine, both by molecular simulations and experimentally, that ten molecules of BSA form a monolayer around the

  17. Nanoparticle albumin-bound paclitaxel combined with cisplatin as the first-line treatment for metastatic esophageal squamous cell carcinoma

    Directory of Open Access Journals (Sweden)

    Shi Y

    2013-05-01

    Full Text Available Yan Shi, Rui Qin, Zhi-Kuan Wang, Guang-Hai DaiDepartment of Multimodality Therapy of Oncology, General Hospital of CPLA, Beijing, People's Republic of ChinaAbstract: Esophageal cancer is a major health hazard in many parts of the world and is often diagnosed late. The objective of this study was to explore the efficacy and safety of nanoparticle albumin-bound paclitaxel (Nab-PTX combined with cisplatin (DDP in patients with metastatic esophageal squamous cell carcinoma (ESCC. Patients with histologically confirmed ESCC were treated with Nab-PTX 250 mg/m2 and DDP 75 mg/m2 intravenously on day 1, every 21 days. Evaluation was performed after every two cycles of therapy and the therapy was continued until disease progression or unacceptable toxicity. From April 2010 to December 2012, 33 patients were enrolled. Ten patients had recurrent and metastatic tumors after surgery and 23 patients were diagnosed with unresectable metastatic disease. Patients received a median of four cycles of therapy (ranging from two to six cycles. Twenty patients achieved partial response and nine patients achieved stable disease; no complete response was observed. The objective response rate was 60.6% and the disease control rate was 87.9%. The median progression-free survival was 6.2 months (95% confidence interval: 4.0 to 8.4 months and the median overall survival was 15.5 months (95% CI: 7.6 to 23.4 months. Only four patients experienced grade 3 adverse events, including vomiting, neutropenia, and sensory neuropathy. The most common adverse events were nausea/vomiting (81.8%, neutropenia (63.6%, leucopenia (48.5%, anemia (24.2% and sensory neuropathy (24.2%. In conclusion, the combination of Nab-PTX and DDP is a highly effective and well-tolerated first-line treatment in metastatic ESCC.Keywords: esophageal squamous cell carcinoma, nanoparticle albumin-bound paclitaxel, chemotherapy, metastasis

  18. Structure and interaction among protein and nanoparticle mixture in solution: Effect of temperature

    International Nuclear Information System (INIS)

    Structure and interaction among globular protein bovine serum albumin (BSA) and silica nanoparticle mixtures in solutions have been studied using small angle Neutron Scattering(SANS) technique by varying the solution temperature, and protein and nanoparticle concentrations. Our study shows that in absence of nanopaticles and up to a moderate temperature (≈75°C), a short-range attraction and in addition a long-range electrostatic repulsion between the protein molecules exist. However, the attractive interaction among BSA increases with the increase of the solution temperature. Above that temperature, fractal structure forms and the fractal structure exist even when the solution temperature is reduced to the initial room temperature (≈30°C). In presence of nanoparticles, fractal structures form even at room temperature by both the protein and nanoparticles. The fractal dimension increases with the increase of the solution temperature and this temperature induced structural transition is irreversible. Variations of nanoparticle concentrations show nearly the same behavior.

  19. Clinical experience with nanoparticle albumin-bound paclitaxel, a novel taxane anticancer agent, and management of adverse events in females with breast cancer

    OpenAIRE

    Takashima,Seiki; KIYOTO, SACHIKO; TAKAHASHI, MINA; Hara, Fumikata; Aogi, Kenjiro; Ohsumi, Shozo; MUKAI, RYOKO; FUJITA, YORIKO

    2015-01-01

    Nanoparticle albumin-bound paclitaxel (nab-paclitaxel) is currently approved in Japan for treatment of breast cancer. However, apart from phase I clinical trials, data regarding Japanese patients are scant. In the present study, the efficacy and safety of nab-paclitaxel therapy were retrospectively analyzed in 22 patients with advanced or metastatic breast cancer who were treated at the National Hospital Organization Shikoku Cancer Center between November 2010 and June 2012. The nab-paclitaxe...

  20. Comparison of Behaviour in Different Liquids and in Cells of Gold Nanorods and Spherical Nanoparticles Modified by Linear Polyethyleneimine and Bovine Serum Albumin

    Directory of Open Access Journals (Sweden)

    Inna A. Pyshnaya

    2014-01-01

    Full Text Available Gold nanorods (GNRs are considered one of the most promising forms of nanoparticles for nanobiotechnology; however, the problem of their toxicity is currently not resolved. We synthesised GNRs, modified with linear polyethyleneimine (PEI-GNRs, and examined their physicochemical and some biological properties in comparison with GNRs modified with BSA and spherical gold nanoparticles (sGNPs modified with the same agents. The influence of the buffer, cell culture media, and serum on hydrodynamic diameter and zeta potential of all GNPs was studied. Simultaneously, the size, shape, and formation of a corona were examined by transmission electron microscopy (TEM. PEI-GNRs and GNPs were nontoxic for BHK-21 and HeLa cells (MTT test. Penetration of all GNPs into BHK-21, melanoma B16, and HeLa cells was examined after 30 min, 3 h, and 24 h of incubation using TEM ultrathin sections. PEI-GNRs and PEI-sGNPs demonstrated fast and active penetration into cells by caveolin-dependent and lipid raft-mediated endocytosis and accumulated in endosomes and lysosomes. BSA-modified GNPs showed prolonged flotation and a significant delay in cell penetration. The results show that the charge of initial NPs determines penetration into cells. Thus, the designed PEI-GNRs were nontoxic and stable in cell culture media and could efficiently penetrate cells.

  1. Nanoparticle fouling and its combination with organic fouling during forward osmosis process for silver nanoparticles removal from simulated wastewater

    Science.gov (United States)

    Zhao, Yanxiao; Wang, Xinhua; Wang, Zhiwei; Li, Xiufen; Ren, Yueping

    2016-01-01

    The increasing and wide application of silver nanoparticles (Ag NPs) has resulted in their appearance in wastewater. In consideration of their potential toxicity and environmental impacts, it is necessary to find effective technology for their removal from wastewater. Here, forward osmosis (FO) membrane was applied for Ag NPs removal from wastewater, and single and combined fouling of nanoparticles and organic macromolecules were further investigated during the FO process. The findings demonstrated that FO membrane can effectively remove Ag NPs from wastewater due to its high rejection performance. Fouling tests indicated that water flux declined appreciably even at the beginning of the single Ag NPs fouling test, and more remarkable flux decline and larger amounts of deposited Ag NPs were observed with an increase of Ag NPs concentration. However, the addition of bovine serum albumin (BSA) could effectively alleviate the FO membrane fouling induced by Ag NPs. The interaction between Ag NPs and BSA was responsible for this phenomenon. BSA can easily form a nanoparticle-protein corona surrounded nanoparticles, which prevented nanoparticles from aggregation due to the steric stabilization mechanism. Furthermore, the interaction between BSA and Ag NPs occurred not only in wastewater but also on FO membrane surface. PMID:27160045

  2. Nanoparticle fouling and its combination with organic fouling during forward osmosis process for silver nanoparticles removal from simulated wastewater

    Science.gov (United States)

    Zhao, Yanxiao; Wang, Xinhua; Wang, Zhiwei; Li, Xiufen; Ren, Yueping

    2016-05-01

    The increasing and wide application of silver nanoparticles (Ag NPs) has resulted in their appearance in wastewater. In consideration of their potential toxicity and environmental impacts, it is necessary to find effective technology for their removal from wastewater. Here, forward osmosis (FO) membrane was applied for Ag NPs removal from wastewater, and single and combined fouling of nanoparticles and organic macromolecules were further investigated during the FO process. The findings demonstrated that FO membrane can effectively remove Ag NPs from wastewater due to its high rejection performance. Fouling tests indicated that water flux declined appreciably even at the beginning of the single Ag NPs fouling test, and more remarkable flux decline and larger amounts of deposited Ag NPs were observed with an increase of Ag NPs concentration. However, the addition of bovine serum albumin (BSA) could effectively alleviate the FO membrane fouling induced by Ag NPs. The interaction between Ag NPs and BSA was responsible for this phenomenon. BSA can easily form a nanoparticle-protein corona surrounded nanoparticles, which prevented nanoparticles from aggregation due to the steric stabilization mechanism. Furthermore, the interaction between BSA and Ag NPs occurred not only in wastewater but also on FO membrane surface.

  3. BSA 500 UOP Course Tutorial / Tutorialrank

    OpenAIRE

    charles

    2015-01-01

    For more course tutorials visit   www.tutorialrank.com   Tutorial Purchased: 4 Times, Rating: A+           BSA 500 Week 1 Learning Team Charter (UOP Course) BSA 500 Week 2 Individual Assignment Virtual Organizations Table Part I (UOP Course) BSA 500 Week 3 Individual Assignment Table 1 Part 2 Virtual Organization (UOP Course) BSA 500 Week 4 Individual Assingment Balance Sheet and Income Statement (UOP Cours...

  4. Gold Nanoparticle-Based Facile Detection of Human Serum Albumin and Its Application as an INHIBIT Logic Gate.

    Science.gov (United States)

    Huang, Zhenzhen; Wang, Haonan; Yang, Wensheng

    2015-05-01

    In this work, a facile colorimetric method is developed for quantitative detection of human serum albumin (HSA) based on the antiaggregation effect of gold nanoparticles (Au NPs) in the presence of HSA. The citrate-capped Au NPs undergo a color change from red to blue when melamine is added as a cross-linker to induce the aggregation of the NPs. Such an aggregation is efficiently suppressed upon the adsorption of HSA on the particle surface. This method provides the advantages of simplicity and cost-efficiency for quantitative detection of HSA with a detection limit of ∼1.4 nM by monitoring the colorimetric changes of the Au NPs with UV-vis spectroscopy. In addition, this approach shows good selectivity for HSA over various amino acids, peptides, and proteins and is qualified for detection of HSA in a biological sample. Such an antiaggregation effect can be further extended to fabricate an INHIBIT logic gate by using HSA and melamine as inputs and the color changes of Au NPs as outputs, which may have application potentials in point-of-care medical diagnosis. PMID:25850684

  5. Interaction between titanium dioxide nanoparticles and human serum albumin revealed by fluorescence spectroscopy in the absence of photoactivation

    Energy Technology Data Exchange (ETDEWEB)

    Sun Wen [Department of Analytical Chemistry, China Pharmaceutical University, Nanjing 210009 (China); Du Yingxiang, E-mail: du_yingxiang@126.co [Key Laboratory of Drug Quality Control and Pharmacovigilance, Ministry of Education, China Pharmaceutical University, No. 24, Tongjiaxiang, Nanjing, Jiangsu 210009 (China) and Department of Analytical Chemistry, China Pharmaceutical University, Nanjing 210009 (China); Chen Jianqiu [Department of Analytical Chemistry, China Pharmaceutical University, Nanjing 210009 (China); Kou Junping; Yu Boyang [Department of Complex Prescription of TCM, China Pharmaceutical University, Nanjing 210009 (China)

    2009-08-15

    Titanium dioxide (TiO{sub 2}) nanoparticles (NPs) are widely used as an important kind of biomaterials. The interaction between TiO{sub 2} (P25) at 20 nm in diameter and human serum albumin (HSA) was studied by fluorescence spectroscopy in this work. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on HSA and its binding constants (K{sub a}) were 2.18+-0.04x10{sup 4}, 0.87+-0.05x10{sup 4}, 0.68+-0.06x10{sup 4} M{sup -1} at 298, 304 and 310 K, respectively. In addition, according to the Van't Hoff equation, the thermodynamic functions standard enthalpy (DELTAH{sup 0}) and standard entropy (DELTAS{sup 0}) for the reaction were calculated to be -75.18+-0.15 kJ mol{sup -1} and -170.11+-0.38 J mol{sup -1} K{sup -1}. These results indicated that TiO{sub 2} NPs bond to HSA mainly by van der Waals force and hydrogen bonding formation in low dielectric media, and the electrostatic interactions cannot be excluded. Furthermore, the effects of common ions on the binding constant of TiO{sub 2} NPs-HSA complex were discussed.

  6. Interaction between titanium dioxide nanoparticles and human serum albumin revealed by fluorescence spectroscopy in the absence of photoactivation

    International Nuclear Information System (INIS)

    Titanium dioxide (TiO2) nanoparticles (NPs) are widely used as an important kind of biomaterials. The interaction between TiO2 (P25) at 20 nm in diameter and human serum albumin (HSA) was studied by fluorescence spectroscopy in this work. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on HSA and its binding constants (Ka) were 2.18±0.04x104, 0.87±0.05x104, 0.68±0.06x104 M-1 at 298, 304 and 310 K, respectively. In addition, according to the Van't Hoff equation, the thermodynamic functions standard enthalpy (ΔH0) and standard entropy (ΔS0) for the reaction were calculated to be -75.18±0.15 kJ mol-1 and -170.11±0.38 J mol-1 K-1. These results indicated that TiO2 NPs bond to HSA mainly by van der Waals force and hydrogen bonding formation in low dielectric media, and the electrostatic interactions cannot be excluded. Furthermore, the effects of common ions on the binding constant of TiO2 NPs-HSA complex were discussed.

  7. Potential-dependent surface denaturation of BSA in acid media

    Czech Academy of Sciences Publication Activity Database

    Paleček, Emil; Ostatná, Veronika

    2009-01-01

    Roč. 134, č. 10 (2009), s. 2076-2080. ISSN 0003-2654 R&D Projects: GA ČR(CZ) GA301/07/0490; GA ČR(CZ) GP202/07/P497; GA AV ČR(CZ) KJB100040901; GA MŠk(CZ) LC06035 Institutional research plan: CEZ:AV0Z50040507; CEZ:AV0Z50040702 Keywords : bovine serum albumin denaturation * chronopotentiometry of BSA Subject RIV: BO - Biophysics Impact factor: 3.272, year: 2009

  8. Preparation, characterization and in vitro cytotoxicity of BSA-based nanospheres containing nanosized magnetic particles and/or photosensitizer

    International Nuclear Information System (INIS)

    This study reports on the preparation, characterization and in vitro toxicity test of a new nano-drug delivery system (NDDS) based on bovine serum albumin (BSA) nanospheres which incorporates surface-functionalized magnetic nanoparticles (MNP) and/or the silicon(IV) phthalocyanine (NzPc). The new NDDS was engineered for use in photodynamic therapy (PDT) combined with hyperthermia (HPT) to address cancer treatment. The BSA-based nanospheres, hosting NzPc, MNP or both (NzPc and MNP), present spherical shape with hydrodynamic average diameter values ranging from 170 to 450 nm and zeta potential of around -23 mV. No difference on the fluorescence spectrum of the encapsulated NzPc was found regardless of the presence of MNP. Time-dependent fluorescence measurements of the encapsulated NzPc revealed a bi-exponential decay for samples incorporating only NzPc and NzPc plus MNP, in the time window ranging from 1.70 to 5.20 ns. The in vitro assay, using human fibroblasts, revealed no cytotoxic effect in all samples investigated, demonstrating the potential of the tested system as a synergistic NDDS.

  9. INTERFACIAL FREE-ENERGY CHANGES OCCURRING DURING BSA ADSORPTION IN SOLUTION DROPLETS ON FEP-TEFLON SURFACES AS MEASURED BY ADSA-P

    NARCIS (Netherlands)

    BUSSCHER, HJ; VANDERVEGT, W; SCHAKENRAAD, JM; VANDERMEI, HC

    1991-01-01

    Axisymmetric drop shape analysis by profile (ADSA-P) was employed to determine the interfacial free energy changes occurring during bovine serum albumin (BSA) adsorption from solution droplets on fluoroethylenepropylene-Teflon (FEP-Teflon). 100-mu-l droplets of BSA solutions on FEP-Teflon were follo

  10. Synthesis of Mn-modified CdTe nanoparticles and their application as fluorescence probe

    International Nuclear Information System (INIS)

    Mn-modified CdTe nanoparticles (NPs) were synthesized via a novel, facile method at low temperature. The modified NPs were directly synthesized in aqueous solution by mixing CdCl2·2.5H2O, fresh NaHTe solution, thioglycolic acid (TGA) and MnCl2·4H2O under suitable conditions. Mn-modified CdTe NPs were evaluated as fluorescence probe for bovine serum albumin (BSA) in aqueous solution. Experiment results showed that the fluorescence emission of Mn-modified CdTe NPs was enhanced significantly by BSA, while other substances exhibited no significant effect on NPs. Under the optimal conditions, the response was linearly proportional to the concentration of BSA ranging from 5.0×10−9 to 7.0×10−7 mol/L with detection limit 5.26×10−10 mol/L. Based on the distinct optical properties of Mn-modified CdTe NPs with BSA, Mn-modified CdTe NPs can be developed as a potential identified fluorescence probe for BSA in aqueous solution. -- Highlights: • Mn-modified CdTe nanoparticles were synthesized via a facile method at low temperature. • The fluorescence properties and morphology of Mn-CdTe nanoparticles were studied clearly. • Mn-CdTe nanoparticles show superior response to the bovine serum albumin molecular on the fluorescence emission. • This detection method was sensitive and provides a wide range of bovine serum albumin concentrations

  11. The inhibition of advanced glycation end-products-induced retinal vascular permeability by silver nanoparticles.

    Science.gov (United States)

    Sheikpranbabu, Sardarpasha; Kalishwaralal, Kalimuthu; Lee, Kyung-Jin; Vaidyanathan, Ramanathan; Eom, Soo Hyun; Gurunathan, Sangiliyandi

    2010-03-01

    The increased permeability of the blood-retinal barrier is known to occur in patients with diabetes, and this defect contributes to retinal edema. This study aimed to determine the effects of silver nanoparticles (Ag-NPs) on advanced glycation end-products (AGEs)-induced endothelial cell permeability. Cultured porcine retinal endothelial cells (PRECs) were exposed to AGE-modified bovine serum albumin (AGE-BSA) and the endothelial cell permeability was detected by measuring the flux of RITC-dextran across the PREC monolayers. We found that AGE-BSA increased the dextran flux across a PREC monolayer and Ag-NPs blocked the solute flux induced by AGE-BSA. In order to understand the underlying signaling mechanism of Ag-NPs on the inhibitory effect of AGE-BSA-induced permeability, we demonstrated that Ag-NPs could inhibit the AGE-BSA-induced permeability via Src kinase pathway. AGE-BSA also increased the PREC permeability by stimulating the expression of intracellular adhesion molecule-1 (ICAM-1) and decreased the expression of occludin and ZO-1. Further, Ag-NPs inhibited the AGE-BSA-induced permeability by increased expression of tight junction proteins occludin and ZO-1, co-incident with an increase in barrier properties of endothelial monolayer. Together, our results indicate that Ag-NPs could possibly act as potent anti-permeability molecule by targeting the Src signaling pathway and tight junction proteins and it offers potential targets to inhibit the ocular related diseases. PMID:19963272

  12. Interactions of two food colourants with BSA: Analysis by Debye-Hückel theory.

    Science.gov (United States)

    Li, Tian; Cheng, Zhengjun; Cao, Lijun; Jiang, Xiaohui; Fan, Lei

    2016-11-15

    We have focused on exploring pH- and ionic strength-modulated binding of acid red 1 (AR1) and acid green 50 (AG50) with bovine serum albumin (BSA) by fluorescence, UV-vis absorption and FTIR spectra. The results implied that the quenching mechanism of BSA-AR1/AG50 system was a static quenching, electrostatic force dominated the formation of BSA-AR1/AG50 complex, and the binding affinity of AR1 was greater than that of AG50 on the subdomain IIA of BSA. Moreover, their true thermodynamic binding constant (Keq), true free energy change (ΔG(0)I→0), and effective charge (ZP) in the anion receptor pocket of BSA were calculated using Debye-Hückel limiting law. The local charge bound by AR1/AG50 rather than the overall or surface charge of BSA played a key role in determining their interaction strength. Besides, the thermal and structural stabilization of BSA was discussed by analyzing the changes of Tm and Hurea without/with the addition of AR1/AG50, respectively. PMID:27283623

  13. Ascorbic Acid and BSA Protein in Solution and Films: Interaction and Surface Morphological Structure

    Directory of Open Access Journals (Sweden)

    Rafael R. G. Maciel

    2013-01-01

    Full Text Available This paper reports on the study of the interactions between ascorbic acid (AA and bovine serum albumin (BSA in aqueous solution as well as in films (BSA/AA films prepared by the layer-by-layer technique. Regarding to solution studies, a hyperchromism (in the range of ultraviolet was found as a function of AA concentration, which suggested the formation of aggregates from AA and BSA. Binding constant, , determined for aggregates from BSA and AA was found to be about 102 M−1, which indicated low affinity of AA with BSA. For the BSA/AA films, it was also noted that the AA adsorption process and surface morphological structures depended on AA concentration. By changing the contact time between the AA and BSA, a hypochromism was revealed, which was associated to decrease of accessibility of solvent to tryptophan due to formation of aggregates. Furthermore, different morphological structures of aggregates were observed, which were attributed to the diffusion-limited aggregation. Since most of studies of interactions of drugs and proteins are performed in solution, the analysis of these processes by using films can be very valuable because this kind of system is able to employ several techniques of investigation in solid state.

  14. Preparation and Optimization Experiment of Docetaxel-loaded Bovine Serum Albumin Nanoparticles%多西紫杉醇白蛋白微球的制备及优化实验研究

    Institute of Scientific and Technical Information of China (English)

    张智舟; 姜守刚; 祖元刚; 赵冬梅; 赵修华; 金晓慧

    2011-01-01

    多西紫杉醇(DT)是唯一应用于临床治疗肿瘤的紫杉醇的衍生物,其水溶性差,制剂中需要加入有机溶剂和助溶剂,而有机溶剂和助溶剂具有刺激性.为减少多西紫杉醇制剂的刺激性,本实验通过去溶剂化-化学交联法制备水溶性多西紫杉醇白蛋白微球.对制备过程中的重要影响因素进行考察,并通过Design-expert软件进行数据优化,最终得优化条件:白蛋白浓度为35mg·mL-1,DT浓度为1.03mg·mL-1,乙醇和水的比例为3:1,乙醇的滴加速度为0.73mL·min-1,搅拌时间为12h,0.2%戊二醛与白蛋白的交联比为2:1.得到的多西紫杉醇白蛋白微球粒径为185nm,载药量为14.4%,成功的解决了其水溶性,为接下来的动物实验、临床应用提供了良好的基础.%Docetaxel ( DT), the only derivative of paclitaxel for clinical application in tumor, is mainly used for the treatment of breast cancer, nonsmall-cell lung cancer, oophoroma, etc. Because of its low solubility, organic solvents and solution adjuvants are always added to the preparation. However, organic solvents and solution adjuvants are pungent. Solubility of docetaxel can be increased by the preparation of docetaxel-loaded bovine serum albumin nanoparticles (DT-BSA-NPs) through desolvation-chemical crosslinking method. In this study, the important factors during preparation were tested, and the optimal conditions were obtained according to the optimized data by Design-expert. These data were as follows: the concentration of albumin was 35 mg · mL-1 , the concentration of DT was 1.03 mg · mL-1, the ratio of ethanol to water was 3:1, the dripping speed of ethanol was 0.73 mL · min-1, the stirring time was 12 h, cross-link ratio of glutaraldehyde and BSA was 2:1. The particle size of the product is 185 nm, and the drug-loading rate is 14.4%. The developed method successfully helped to improve the water-solubility of docetaxel and therefore provided a good foundation for the animal

  15. Albumin Test

    Science.gov (United States)

    ... be limited. Home Visit Global Sites Search Help? Albumin Share this page: Was this page helpful? Also known as: ALB Formal name: Albumin, serum Related tests: Liver Panel , Comprehensive Metabolic Panel , ...

  16. Enhanced Response of a Proteinase K-Based Conductometric Biosensor Using Nanoparticles

    Directory of Open Access Journals (Sweden)

    Wided Nouira

    2014-07-01

    Full Text Available Proteinases are involved in a multitude of important physiological processes, such as protein metabolism. For this reason, a conductometric enzyme biosensor based on proteinase K was developed using two types of nanoparticles (gold and magnetic. The enzyme was directly adsorbed on negatively charged nanoparticles and then deposited and cross-linked on a planar interdigitated electrode (IDE. The biosensor was characterized with bovine serum albumin (BSA as a standard protein. Higher sensitivity was obtained using gold nanoparticles. The linear range for BSA determination was then from 0.5 to 10 mg/L with a maximum response of 154 µs. These results are greater than that found without any nanoparticles (maximum response of 10 µs. The limit of detection (LOD was 0.3 mg/L. An inter-sensor reproducibility of 3.5% was obtained.

  17. BINDING EFFICACY AND ELUCIDATION OF QUANTITATIVE STRUCTURE ACTIVITY RELATIONSHIP OF ACETANILIDE AND ITS DERIVATIVES WITH BOVINE SERUM ALBUMIN AND THEIR INHIBITION AGAINST COX1

    Directory of Open Access Journals (Sweden)

    Dr. Violet Dhayabaran et al

    2012-09-01

    Full Text Available Serum albumins are the most abundant proteins in plasma with many physiological functions. Among them, BSA has a wide range of functions involving the binding, transport and delivery of fatty acids, porphyrins, bilirubin, steroids, etc and it is home to specific binding sites for metals, pharmaceuticals and dyes. Recently, nanotechnology has become a popular term in the current science and technology. Nanotechnology has been introduced for the food and drug industry, including encapsulations and delivery systems. BSA nanoparticles were prepared and their binding efficacy with the available analgesics such as acetanilide and its derivatives were studied. The value of apparent rate constant Kapp from the interaction between acetanilide and BSA by UV visible spectroscopic and fluorescence technique was found to be 2.294X106. The quenching rate constant of BSA-Acetanilide was found to be 1.0345X1015M-1 S-1. There are two binding sites in BSA for acetanilide. A QSAR study was performed for the different analgesics. Inhibition of Acetanilide and its derivatives with the Cyclooxygenase (COX 1 was studied using docking mechanism. The electro chemical behavior of acetanilide is studied and it is found to be reversible.

  18. Human serum albumin as protecting agent of silver nanoparticles: role of the protein conformation and amine groups in the nanoparticle stabilization

    Energy Technology Data Exchange (ETDEWEB)

    Alarcon, Emilio I.; Bueno-Alejo, Carlos J.; Noel, Christopher W.; Stamplecoskie, Kevin G. [Centre for Catalysis Research and Innovation, University of Ottawa, Department of Chemistry (Canada); Pacioni, Natalia L. [Facultad de Ciencias Quimicas, Universidad Nacional de Cordoba, INFIQC, Departamento de Quimica Organica (Argentina); Poblete, Horacio [Center for Bioinformatics and Molecular Simulations, Universidad de Talca (Chile); Scaiano, J. C., E-mail: tito@photo.chem.uottawa.ca [Centre for Catalysis Research and Innovation, University of Ottawa, Department of Chemistry (Canada)

    2013-01-15

    Thermally denatured human serum albumin interacts with {approx}3.0 nm spherical AgNP enhancing the fluorescence of Trp-214 at large protein/nanoparticle ratios. However, using native HSA, no changes in the emission were observed. The observation is likely due to differences between native and denatured protein packing resulting from protein corona formation. We have also found that NH{sub 2} blocking of the protein strongly affects the ability of the protein to protect AgNP from different salts/ions such as NaCl, PBS, Hank's buffer, Tris-HCl, MES, and DMEM. Additionally, AgNP can be readily prepared in aqueous solutions by a photochemical approach employing HSA as an in situ protecting agent. The role of the protein in this case is beyond that of protecting agent; thus, Ag{sup +} ions and I-2959 complexation within the protein structure also affects the efficiency of AgNP formation. Blocking NH{sub 2} in HSA modified the AgNP growth profile, surface plasmon band shape, and long-term stability suggesting that amine groups are directly involved in the formation and post-stabilization of AgNP. In particular, AgNP size and shape are extensively influenced by NH{sub 2} blocking, leading primarily to cubes and plates with sizes around 5-15 nm; in contrast, spherical monodisperse 4.0 nm AgNP are observed for native HSA. The nanoparticles prepared by this protocol are non-toxic in primary cells and have remarkable antibacterial properties. Finally, surface plasmon excitation of native HSA-AgNP promoted loss of protein conformation in just 5 min, suggesting that plasmon heating causes protein denaturation using continuous light sources such as commercial LED.

  19. Human serum albumin as protecting agent of silver nanoparticles: role of the protein conformation and amine groups in the nanoparticle stabilization

    International Nuclear Information System (INIS)

    Thermally denatured human serum albumin interacts with ∼3.0 nm spherical AgNP enhancing the fluorescence of Trp-214 at large protein/nanoparticle ratios. However, using native HSA, no changes in the emission were observed. The observation is likely due to differences between native and denatured protein packing resulting from protein corona formation. We have also found that NH2 blocking of the protein strongly affects the ability of the protein to protect AgNP from different salts/ions such as NaCl, PBS, Hank’s buffer, Tris–HCl, MES, and DMEM. Additionally, AgNP can be readily prepared in aqueous solutions by a photochemical approach employing HSA as an in situ protecting agent. The role of the protein in this case is beyond that of protecting agent; thus, Ag+ ions and I-2959 complexation within the protein structure also affects the efficiency of AgNP formation. Blocking NH2 in HSA modified the AgNP growth profile, surface plasmon band shape, and long-term stability suggesting that amine groups are directly involved in the formation and post-stabilization of AgNP. In particular, AgNP size and shape are extensively influenced by NH2 blocking, leading primarily to cubes and plates with sizes around 5–15 nm; in contrast, spherical monodisperse 4.0 nm AgNP are observed for native HSA. The nanoparticles prepared by this protocol are non-toxic in primary cells and have remarkable antibacterial properties. Finally, surface plasmon excitation of native HSA-AgNP promoted loss of protein conformation in just 5 min, suggesting that plasmon heating causes protein denaturation using continuous light sources such as commercial LED.

  20. Enhanced performance of macrophage-encapsulated nanoparticle albumin-bound-paclitaxel in hypo-perfused cancer lesions

    Science.gov (United States)

    Leonard, Fransisca; Curtis, Louis T.; Yesantharao, Pooja; Tanei, Tomonori; Alexander, Jenolyn F.; Wu, Min; Lowengrub, John; Liu, Xuewu; Ferrari, Mauro; Yokoi, Kenji; Frieboes, Hermann B.; Godin, Biana

    2016-06-01

    Hypovascularization in tumors such as liver metastases originating from breast and other organs correlates with poor chemotherapeutic response and higher mortality. Poor prognosis is linked to impaired transport of both low- and high-molecular weight drugs into the lesions and to high washout rate. Nanoparticle albumin-bound-paclitaxel (nAb-PTX) has demonstrated benefits in clinical trials when compared to paclitaxel and docetaxel. However, its therapeutic efficacy for breast cancer liver metastasis is disappointing. As macrophages are the most abundant cells in the liver tumor microenvironment, we design a multistage system employing macrophages to deliver drugs into hypovascularized metastatic lesions, and perform in vitro, in vivo, and in silico evaluation. The system encapsulates nAb-PTX into nanoporous biocompatible and biodegradable multistage vectors (MSV), thus promoting nAb-PTX retention in macrophages. We develop a 3D in vitro model to simulate clinically observed hypo-perfused tumor lesions surrounded by macrophages. This model enables evaluation of nAb-PTX and MSV-nab PTX efficacy as a function of transport barriers. Addition of macrophages to this system significantly increases MSV-nAb-PTX efficacy, revealing the role of macrophages in drug transport. In the in vivo model, a significant increase in macrophage number, as compared to unaffected liver, is observed in mice, confirming the in vitro findings. Further, a mathematical model linking drug release and retention from macrophages is implemented to project MSV-nAb-PTX efficacy in a clinical setting. Based on macrophage presence detected via liver tumor imaging and biopsy, the proposed experimental/computational approach could enable prediction of MSV-nab PTX performance to treat metastatic cancer in the liver.Hypovascularization in tumors such as liver metastases originating from breast and other organs correlates with poor chemotherapeutic response and higher mortality. Poor prognosis is linked to

  1. Targeted chemotherapy with nanoparticle albumin-bound paclitaxel (nab-paclitaxel) in metastatic breast cancer: which benefit for which patients?

    Science.gov (United States)

    Palumbo, Raffaella; Sottotetti, Federico; Bernardo, Antonio

    2016-01-01

    The therapeutic goals in metastatic breast cancer (MBC) remain palliative in nature, aimed at controlling symptoms, improving or maintaining quality of life and prolonging survival. The advent of new drugs and new formulations of standard agents has led to better outcomes in patients with advanced or metastatic disease. These developments have also allowed a tailored therapeutic approach, in which the molecular biology of the tumour, the treatment history, and patient attitudes are taken into account in the decision-making process. Targeting drug delivery to the tumour is a promising mean of increasing the therapeutic index of highly active agents such as the taxanes, and nanoparticle albumin-bound paclitaxel (nab-paclitaxel), the first nanotechnology-based drug developed in cancer treatment, is one such advance. Data from randomized trials support the efficacy of single-agent nab-paclitaxel as first-line and further treatment lines in MBC at the registered 3-weekly schedule of 260 mg/m2, but emerging evidence suggests its activity as a weekly regimen or combined with other agents in various clinical scenarios. Thus, nab-paclitaxel seems to offer flexibility in terms of dosing schedules, allowing physicians to tailor the dose according to different clinical situations. This paper reviews the clinical trial background for nab-paclitaxel in MBC, focusing on specific ‘difficult-to-treat’ patient populations, such as taxane-pretreated or elderly women, as well as those with triple-negative, HER2-positive and poor-prognostic-factors disease. Moving beyond evidence-based information, ‘real life’ available experiences are also discussed with the aim of providing an update for daily clinical practice. PMID:27239239

  2. Effects of Gold Salt Speciation and Structure of Human and Bovine Serum Albumin on the Synthesis and Stability of Gold Nanostructures

    Science.gov (United States)

    Miranda, Érica; Tofanello, Aryane; Brito, Adrianne; Lopes, David; Giacomelli, Fernando; Albuquerque, Lindomar; Costa, Fanny; Ferreira, Fabio; Araujo-Chaves, Juliana; de Castro, Carlos; Nantes, Iseli

    2016-03-01

    The present study aimed to investigate the influence of albumin structure and gold speciation on the synthesis of gold nanoparticles (GNPs). The strategy of synthesis was the addition of HAuCl4 solutions at different pH values (3-12) to solutions of human and bovine serum albumins (HSA and BSA) at the same corresponding pH values. Different pH values influence the GNP synthesis due to gold speciation. Besides the inherent effect of pH on the native structure of albumins, the use N-ethylmaleimide (NEM)-treated and heat-denaturated forms of HSA and BSA provided additional insights about the influence of protein structure, net charge, and thiol group approachability on the GNP synthesis. NEM treatment, heating, and the extreme values of pH promoted loss of the native albumin structure. The formation of GNPs indicated by the appearance of surface plasmon resonance (SPR) bands became detectable from fifteen days of the synthesis processes that were carried out with native, NEM-treated and heat-denaturated forms of HSA and BSA, exclusively at pH 6 and 7. After two months of incubation, SPR band was also detected for all synthesis carried out at pH 8.0. The mean values of the hydrodynamic radius (RH) were 24 and 34 nm for GNPs synthesized with native HSA and BSA, respectively. X-ray diffraction (XRD) revealed crystallites of 13 nm. RH, XRD, and zeta potential values were consistent with GNP capping by the albumins. However, the GNPs produced with NEM-treated and heat-denaturated albumins exhibited loss of protein capping by lowering the ionic strength. This result suggests a significant contribution of non-electrostatic interactions of albumins with the GNP surface, in these conditions. The denaturation of proteins exposes hydrophobic groups to the solvent, and these groups could interact with the gold surface. In these conditions, the thiol blockage or oxidation, the latter probably favored upon heating, impaired the formation of a stable capping by thiol coordination

  3. Interaction between fasudil hydrochloride and bovine serum albumin: spectroscopic study.

    Science.gov (United States)

    Yu, Xianyong; Jiang, Bingfei; Xun, Caifang; Yao, Qing

    2016-06-01

    The interaction between fasudil hydrochloride (FSD) and bovine serum albumin (BSA) was investigated using fluorescence and ultraviolet spectroscopy under imitated physiological conditions. The Stern-Volmer quenching model has been successfully applied and the results revealed that FSD could quench the intrinsic fluorescence of BSA effectively via static quenching. The binding constants and binding sites for the BSA-FSD system were evaluated. The corresponding thermodynamic parameters obtained at different temperatures indicated that hydrophobic force played a major role in the interaction of FSD and BSA. The distance between the donor (BSA) and the acceptor (FSD) was obtained according to fluorescence resonance energy transfer (FRET). Synchronous fluorescence spectroscopy and FT-IR spectra showed that the conformation of BSA was changed in the presence of FSD. Copyright © 2015 John Wiley & Sons, Ltd. PMID:26554343

  4. BSA/HSA ratio modulates the properties of Ca(2+)-induced cold gelation scaffolds.

    Science.gov (United States)

    Ribeiro, Artur; Volkov, Vadim; Oliveira, Mariana B; Padrão, Jorge; Mano, João F; Gomes, Andreia C; Cavaco-Paulo, Artur

    2016-08-01

    An effective tissue engineering approach requires adjustment according to the target tissue to be engineered. The possibility of obtaining a protein-based formulation for the development of multivalent tunable scaffolds that can be adapted for several types of cells and tissues is explored in this work. The incremental substitution of bovine serum albumin (BSA) by human serum albumin (HSA), changing the scaffolds' hydrophilic/hydrophobic ratio, on a previously optimized scaffold formulation resulted in a set of uniform porous scaffolds with different physical properties and associated cell proliferation profile along time. There was a general trend towards an increase in hydrophilicity, swelling degree and in vitro degradation of the scaffolds with increasing replacement of BSA by HAS. The set of BSA/HSA scaffolds presented distinct values for the storage (elastic) modulus and loss factor which were similar to those described for different native tissues such as bone, cartilage, muscle, skin and neural tissue. The preferential adhesion and proliferation of skin fibroblasts on the BSA25%HSA75% and HSA100% scaffolds, as predicted by their viscoelastic properties, demonstrate that the BSA/HSA scaffold formulation is promising for the development of scaffolds that can be tuned according to the tissue to be repaired and restored. PMID:27156695

  5. Urine Albumin and Albumin/ Creatinine Ratio

    Science.gov (United States)

    ... limited. Home Visit Global Sites Search Help? Urine Albumin and Albumin/Creatinine Ratio Share this page: Was this page ... known as: Microalbumin; ACR; UACR Formal name: Urine Albumin; Albumin-to-Creatinine Ratio Related tests: Albumin ; Creatinine ; ...

  6. Ultrastable BSA-capped gold nanoclusters with a polymer-like shielding layer against reactive oxygen species in living cells

    Science.gov (United States)

    Zhou, Wenjuan; Cao, Yuqing; Sui, Dandan; Guan, Weijiang; Lu, Chao; Xie, Jianping

    2016-05-01

    The prevalence of reactive oxygen species (ROS) production and the enzyme-containing intracellular environment could lead to the fluorescence quenching of bovine serum albumin (BSA)-capped gold nanoclusters (AuNCs). Here we report an efficient strategy to address this issue, where a polymer-like shielding layer is designed to wrap around the Au core to significantly improve the stability of AuNCs against ROS and protease degradation. The key of our design is to covalently incorporate a thiolated AuNC into the BSA-AuNC via carbodiimide-activated coupling, leading to the formation of a AuNC pair inside the cross-linked BSA molecule. The as-designed paired AuNCs in BSA (or BSA-p-AuNCs for short) show improved performances in living cells.The prevalence of reactive oxygen species (ROS) production and the enzyme-containing intracellular environment could lead to the fluorescence quenching of bovine serum albumin (BSA)-capped gold nanoclusters (AuNCs). Here we report an efficient strategy to address this issue, where a polymer-like shielding layer is designed to wrap around the Au core to significantly improve the stability of AuNCs against ROS and protease degradation. The key of our design is to covalently incorporate a thiolated AuNC into the BSA-AuNC via carbodiimide-activated coupling, leading to the formation of a AuNC pair inside the cross-linked BSA molecule. The as-designed paired AuNCs in BSA (or BSA-p-AuNCs for short) show improved performances in living cells. Electronic supplementary information (ESI) available: Detailed experimental materials, apparatus, experimental procedures and characterization data. See DOI: 10.1039/c6nr02178f

  7. An in vitro and in vivo study of gemcitabine-loaded albumin nanoparticles in a pancreatic cancer cell line

    Directory of Open Access Journals (Sweden)

    Yu XZ

    2015-10-01

    Full Text Available Xinzhe Yu,1,* Yang Di,2,* Chao Xie,3 Yunlong Song,4 Hang He,2 Hengchao Li,1 Xinming Pu,5 Weiyue Lu,3 Deliang Fu,2 Chen Jin1 1Pancreatic Surgery Department, Huashan Hospital, 2Pancreatic Disease Institute, Fudan University, 3School of Pharmacy & Key Laboratory of Smart Drug Delivery, Fudan University, 4School of Pharmacy, The Second Military Medical University, 5The State Key Laboratory of Molecular Engineering of Polymers, Department of Macromolecular Science, Fudan University, Shanghai, People’s Republic of China *These authors contributed equally to this work Background and objectives: Gemcitabine (Gem is far from satisfactory as the first-line regimen for pancreatic cancer, and the emergence of albumin nanoparticles offers new hope for the delivery of Gem. In this study, Gem-loaded human serum albumin nanoparticles (Gem-HSA-NPs were successfully synthesized, characterized, and tested on a BxPC-3 cell line both in vitro and in vivo.Materials and methods: 4-N-myristoyl-gemcitabine (Gem-C14 was obtained first by coupling myristoyl with the 4-amino group of Gem. The Gem-HSA-NPs were then prepared by nanoparticle albumin-bound technology and characterized for particle size, zeta potential, morphology, encapsulation efficiency, drug-loading efficiency, and release characteristics. Using both in vitro and in vivo studies, Gem-C14 and Gem-HSA-NPs were tested on the human pancreatic cancer cell line BxPC-3.Results: Gem-HSA-NPs showed an average particle size of 150±27 nm, and with an encapsulation rate of 82.99%±3.5% and a drug-loading rate of 10.42%±3.5%, they exhibited a favorable controlled- and sustained-release nature. In in vitro, Gem-C14 was equivalent in cytotoxicity to Gem. In in vivo, the Gem-HSA-NPs exhibited the strongest inhibitory effect on tumor growth but the lowest toxicity among the four groups.Conclusion: The enhanced in vivo efficacy of Gem-HSA-NPs toward the pancreatic cancer cell line suggests their potential role for use

  8. Controlled release of bovine serum albumin from hydroxyapatite microspheres for protein delivery system

    International Nuclear Information System (INIS)

    Desorption behavior of a model protein (bovine serum albumin, BSA) on commercial hydroxyapatite (HAp) microspheres and its control were investigated for protein delivery system. The desorption behavior related strongly to the phosphate concentration in phosphate buffer solution: the amount of desorbed BSA increased when the phosphate concentration increased. In physiological buffer solution, which contains 10 mM phosphate, the initial burst release of BSA was observed: 70% of BSA was rapidly desorbed after 0.5 h, and 80% after 24 h. In contrast, the extremely low release profile of BSA was observed in distilled water. For the controlled release of BSA in physiological condition, the BSA-loaded HAp microspheres were encapsulated with a biodegradable polymer, poly(lactic acid-co-glycolic acid) (PLGA) by a solid-in oil-in water (S/O/W) emulsion solvent evaporation method. The initial burst was significantly reduced, and the BSA release was remarkably prolonged by the encapsulation

  9. Human serum albumin nanoparticles as an efficient noscapine drug delivery system for potential use in breast cancer: preparation and in vitro analysis

    Directory of Open Access Journals (Sweden)

    Safaa Sebak

    2010-09-01

    Full Text Available Safaa Sebak, Maryam Mirzaei, Meenakshi Malhotra, Arun Kulamarva, Satya PrakashBiomedical Technology and Cell Therapy Research Laboratory, Department of Biomedical Engineering, Faculty of Medicine, McGill University, Montreal, Quebec, CanadaAbstract: Drug delivery systems such as nanoparticles can provide enhanced efficacy for ­anticancer agents. Noscapine, a widely used cough suppressant for decades has recently been shown to cause significant inhibition and regression of tumor volumes without any detectable ­toxicity in cells or tissues. Nanoparticles made of human serum albumin (HSA represent ­promising strategy for targeted drug delivery to tumor cells by enhancing the drug’s bioavailability and distribution, and reducing the body’s response towards drug resistance. In the ­present study, we report for the first time the incorporation and delivery of noscapine-loaded HSA nanoparticles to tumor cells. The nanoparticles were designed and optimized to achieve a particle size in the range of 150–300 nm with a drug-loading efficiency of 85%–96%. The nanoparticles were evaluated in vitro for their anticancer activity and efficacy on breast cancer cells.Keywords: HSA, encapsulation, microcapsule, nanomedicine, nanotechnology, tumor volumes

  10. Ultrasound-targeted transfection of tissue-type plasminogen activator gene carried by albumin nanoparticles to dog myocardium to prevent thrombosis after heart mechanical valve replacement

    Directory of Open Access Journals (Sweden)

    Ji J

    2012-06-01

    Full Text Available Ji Jun, Ji Shang-Yi, Yang Jian-An, He Xia, Yang Xiao-Han, Ling Wen-Ping, Chen Xiao-LingDepartment of Pathology and Cardiovascular Surgery, Shenzhen Sun Yat-Sen Cardiovascular Hospital, Shenzhen, Guangdong, People's Republic of ChinaBackground: There are more than 300,000 prosthetic heart valve replacements each year worldwide. These patients are faced with a higher risk of thromboembolic events after heart valve surgery and long-term or even life-long anticoagulative and antiplatelet therapies are necessary. Some severe complications such as hemorrhaging or rebound thrombosis can occur when the therapy ceases. Tissue-type plasminogen activator (t-PA is a thrombolytic agent. One of the best strategies is gene therapy, which offers a local high expression of t-PA over a prolonged time period to avoid both systemic hemorrhaging and local rebound thrombosis. There are some issues with t-PA that need to be addressed: currently, there is no up-to-date report on how the t-PA gene targets the heart in vivo and the gene vector for t-PA needs to be determined.Aims: To fabricate an albumin nano-t-PA gene ultrasound-targeted agent and investigate its targeting effect on prevention of thrombosis after heart mechanic valve replacement under therapeutic ultrasound.Methods: A dog model of mechanical tricuspid valve replacement was constructed. A highly expressive t-PA gene plasmid was constructed and packaged by nanoparticles prepared with bovine serum albumin. This nanopackaged t-PA gene plasmid was further cross-linked to ultrasonic microbubbles prepared with sucrose and bovine serum albumin to form the ultrasonic-targeted agent for t-PA gene transfection. The agent was given intravenously followed by a therapeutic ultrasound treatment (1 MHz, 1.5 w/cm2, 10 minutes of the heart soon after valve replacement had been performed. The expression of t-PA in myocardium was detected with multiclonal antibodies to t-PA by the indirect immunohistochemical method

  11. Design and characterization of protein-quercetin bioactive nanoparticles

    Directory of Open Access Journals (Sweden)

    Leng Xiaojing

    2011-05-01

    Full Text Available Abstract Background The synthesis of bioactive nanoparticles with precise molecular level control is a major challenge in bionanotechnology. Understanding the nature of the interactions between the active components and transport biomaterials is thus essential for the rational formulation of bio-nanocarriers. The current study presents a single molecule of bovine serum albumin (BSA, lysozyme (Lys, or myoglobin (Mb used to load hydrophobic drugs such as quercetin (Q and other flavonoids. Results Induced by dimethyl sulfoxide (DMSO, BSA, Lys, and Mb formed spherical nanocarriers with sizes less than 70 nm. After loading Q, the size was further reduced by 30%. The adsorption of Q on protein is mainly hydrophobic, and is related to the synergy of Trp residues with the molecular environment of the proteins. Seven Q molecules could be entrapped by one Lys molecule, 9 by one Mb, and 11 by one BSA. The controlled releasing measurements indicate that these bioactive nanoparticles have long-term antioxidant protection effects on the activity of Q in both acidic and neutral conditions. The antioxidant activity evaluation indicates that the activity of Q is not hindered by the formation of protein nanoparticles. Other flavonoids, such as kaempferol and rutin, were also investigated. Conclusions BSA exhibits the most remarkable abilities of loading, controlled release, and antioxidant protection of active drugs, indicating that such type of bionanoparticles is very promising in the field of bionanotechnology.

  12. Exceptional Response to Nanoparticle Albumin-Bound Paclitaxel and Gemcitabine in a Patient with a Refractory Adenocarcinoma of the Ampulla of Vater.

    Science.gov (United States)

    Kapp, Markus; Kosmala, Aleksander; Kircher, Stefan; Luber, Verena; Kunzmann, Volker

    2016-01-01

    Ampullary carcinoma is a rare tumor and evidence on the treatment of recurrent metastatic disease is scarce. We report the case of a 60-year-old patient with an R0-resected node-positive adenocarcinoma of the papilla of Vater of an initially diagnosed intestinal subtype who developed pulmonary metastases 2 months after adjuvant gemcitabine chemotherapy and, subsequently, liver metastases. Palliative combination chemotherapy with standard regimens for intestinal-type adenocarcinoma (FOLFOX and FOLFIRI) failed. However, subsequent combination chemotherapy with nanoparticle albumin-bound paclitaxel and gemcitabine, a regimen with proven efficacy in metastatic adenocarcinoma of the pancreas, resulted in a durable, very good partial remission. Treatment was manageable and well tolerated. Primary tumor and metastatic tissue were reassessed by immunohistochemistry and had to be reclassified to a mixed phenotype containing predominant elements of the pancreatobiliary subtype. Our case suggests that combination chemotherapy with nanoparticle albumin-bound paclitaxel and gemcitabine could represent a promising option for the treatment of this rare disease and warrants further investigation within controlled clinical trials. Moreover, thorough characterization of ampullary carcinomas by histomorphology and additional immunohistochemistry should become mandatory in order to start a chemotherapeutic regimen tailored for the definitive subtype. PMID:26933414

  13. Templated biomineralization of Au nanoplates under bovine serum albumin Langmuir monolayers

    International Nuclear Information System (INIS)

    Au nanoplates were generated by spontaneous reduction of chloroaurate ions (AuCl4-) under bovine serum albumin (BSA) Langmuir monolayers at room temperature. The structure of the resulting Au particulates was analyzed by means of scanning electron microscopy (SEM), transmission electron microscopy (TEM), X-ray diffraction (XRD), selected-area electron diffraction (SAED), and high resolution transmission electron microscopy (HRTEM). The results showed that BSA provided dual functions for both reducing Au3+ ions and directing anisotropic growth of Au particles into plate-like structure as well. Amorphous Au particulates were obtained firstly in a relatively short reaction time, and then anisotropic Au nanoparticles were generated at extended reaction durations. The triangular Au nanoplates oriented along (1 1 1) basal planes were obtained via the reduction of chloroaurate ions by BSA with a relatively longer reaction duration. The present research provides a biological route to produce single-crystalline gold nanoplates with a wide variety of applications, and it also verifies that the interaction between protein/peptide and gold ions/surface may be used advantageously for green chemical synthesis of nanogold. Hopefully, this would contribute to promote genuine green biomimetic synthesis of nanomaterials with prescribed geometrical features where rationally designed multifunctional peptides are preferred.

  14. Investigation on the interaction between bovine serum albumin and 2,2-diphenyl-1-picrylhydrazyl

    Energy Technology Data Exchange (ETDEWEB)

    Li, Xiangrong [Department of Chemistry, School of Basic Medicine, Xinxiang Medical University, Xinxiang, Henan 453003 (China); Chen, Dejun; Wang, Gongke [School of Chemistry and Chemical Engineering, Key Laboratory of Green Chemical Media and Reactions, Ministry of Education, Henan Normal University, 46 Jian-she Road, Mu Ye District, Xinxiang, Henan 453007 (China); Lu, Yan, E-mail: 1842457577@qq.com [School of Chemistry and Chemical Engineering, Key Laboratory of Green Chemical Media and Reactions, Ministry of Education, Henan Normal University, 46 Jian-she Road, Mu Ye District, Xinxiang, Henan 453007 (China)

    2014-12-15

    Albumin represents a very abundant and important circulating antioxidant in plasma. In this paper, the ability of bovine serum albumin (BSA) to scavenge 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical has been investigated using UV–vis absorption spectra. The result shows that the antioxidant activity of BSA against DPPH radical is similar to glutathione and the value of IC{sub 50} is 5.153×10{sup −5} mol L{sup −1}. The interaction between BSA and DPPH has been investigated without or with the eight popular antioxidants (L-ascorbic acid, α-tocopherol, glutathione, melatonin, (+)-catechin hydrate, procyanidine B3, β-carotene and astaxanthin) by means of fluorescence spectroscopy and circular dichroism (CD) spectroscopy. The fluorescence experiments show that DPPH quenches the fluorescence intensity of BSA through a static mechanism. The quenching process of DPPH with BSA is easily affected by the eight antioxidants, however, they cannot change the quenching mechanism of DPPH with BSA. Additionally, as shown by synchronous fluorescence spectroscopy and CD, DPPH may induce conformational and microenvironmental changes of BSA. - Highlights: • The antioxidant activity of BSA against DPPH is similar to glutathione. • DPPH can quench the fluorescence of BSA through a static quenching. • One molecule of DPPH radical reduced by one molecule of BSA. • The eight antioxidants cannot change the quenching mechanism of DPPH with BSA. • The binding parameters are decreased by the introduction of the eight antioxidants.

  15. Investigation on the interaction between bovine serum albumin and 2,2-diphenyl-1-picrylhydrazyl

    International Nuclear Information System (INIS)

    Albumin represents a very abundant and important circulating antioxidant in plasma. In this paper, the ability of bovine serum albumin (BSA) to scavenge 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical has been investigated using UV–vis absorption spectra. The result shows that the antioxidant activity of BSA against DPPH radical is similar to glutathione and the value of IC50 is 5.153×10−5 mol L−1. The interaction between BSA and DPPH has been investigated without or with the eight popular antioxidants (L-ascorbic acid, α-tocopherol, glutathione, melatonin, (+)-catechin hydrate, procyanidine B3, β-carotene and astaxanthin) by means of fluorescence spectroscopy and circular dichroism (CD) spectroscopy. The fluorescence experiments show that DPPH quenches the fluorescence intensity of BSA through a static mechanism. The quenching process of DPPH with BSA is easily affected by the eight antioxidants, however, they cannot change the quenching mechanism of DPPH with BSA. Additionally, as shown by synchronous fluorescence spectroscopy and CD, DPPH may induce conformational and microenvironmental changes of BSA. - Highlights: • The antioxidant activity of BSA against DPPH is similar to glutathione. • DPPH can quench the fluorescence of BSA through a static quenching. • One molecule of DPPH radical reduced by one molecule of BSA. • The eight antioxidants cannot change the quenching mechanism of DPPH with BSA. • The binding parameters are decreased by the introduction of the eight antioxidants

  16. Tailor-made Au-Ag core–shell nanoparticle 2D arrays on protein-coated graphene oxide with assembly enhanced antibacterial activity

    International Nuclear Information System (INIS)

    Water-dispersible two-dimensional (2D) assemblies of Au-Ag core–shell nanoparticles are obtained through a highly selective electroless silver deposition on pre-assembled gold nanoparticles on bovine serum albumin (BSA)-coated graphene oxide (BSA-GO). While neither BSA-GO nor AuNP-decorated BSA-GO shows any antibacterial ability, the silver-coated GO-Au nanosheets (namely GO-Au-Ag) exhibit an enhanced antibacterial activity against Gram-negative Escherichia coli (E. coli) bacteria, superior to unassembled Au-Ag nanoparticles and even ionic Ag. Such an improvement may be attributed to the increased local concentration of silver nanoparticles around a bacterium and a polyvalent interaction with the bacterial surface. In addition, the colloidal stability of this novel nano-antimicrobial against the formation of random nanoparticle aggregates guarantees a minimized activity loss of the Au-Ag nanoparticles. The antibacterial efficacy of GO-Au-Ag is less sensitive to the existence of Cl−, in comparison with silver ions, providing another advantage for wound dressing applications. Our research unambiguously reveals a strong and very specific interaction between the GO-Au-Ag nanoassembly and E. coli, which could be an important clue toward a rational design, synthesis and assembly of innovative and highly active antibacterial nanomaterials. (paper)

  17. Electric Field-induced Conformational Transition of Bovine Serum Albumin from α -helix to β -sheet

    Institute of Scientific and Technical Information of China (English)

    2000-01-01

    The irreversible conformational transition of bovine serum albumin (BSA) from α -helix to β -sheet, induced by electric field near the electrode surface, was monitored by circular dichroism (CD) with a long optical path thin layer cell (LOPTLC).

  18. Studies on interaction between flavonoids and bovine serum albumin by spectral methods

    International Nuclear Information System (INIS)

    The interaction between three kinds of flavonoids and bovine serum albumin (BSA) was investigated by fluorescence and UV-vis absorption spectrometry. The results indicated that flavonoids have strong ability to quench the intrinsic fluorescence of BSA by forming complexes. The binding constants, number of binding sites, thermodynamic parameters and energy transfer mechanisms were also investigated. Conformation change of BSA was observed from synchronous, three-dimensional fluorescence and circular dichroism spectrum.

  19. Binding of dihydromyricetin and its metal ion complexes with bovine serum albumin

    OpenAIRE

    Guo, Qingquan; Yuan, Juan; Zeng, Jinhua

    2014-01-01

    The binding mechanisms of the interaction of three dihydromyricetin (DMY)–metal complexes (DMY–Cu (II) complex, DMY–Mn (II) complex, DMY–Zn (II) complex) and DMY with bovine serum albumin (BSA) were investigated using fluorescence and ultraviolet spectroscopy at different temperatures. The results indicated some differences in the binding process between different DMY–metal complexes and BSA compared with that of free DMY. All of the complexes and DMY quenched the fluorescence of BSA based on...

  20. Peroxidase mediated conjugation of corn fibeer gum and bovine serum albumin to improve emulsifying properties

    Science.gov (United States)

    The emulsifying properties of corn fiber gum (CFG), a naturally-occurring polysaccharide protein complex, were improved by kinetically controlled formation of hetero-covalent linkages with bovine serum albumin (BSA), using horseradish peroxidase. The formation of hetero-crosslinked CFG-BSA conjugate...

  1. Investigation of the Interaction of Naringin Palmitate with Bovine Serum Albumin: Spectroscopic Analysis and Molecular Docking

    OpenAIRE

    Zhang, Xia; Li, Lin; Xu, Zhenbo; Liang, Zhili; Su, Jianyu; Huang, Jianrong; Li, Bing

    2013-01-01

    Background Bovine serum albumin (BSA) contains high affinity binding sites for several endogenous and exogenous compounds and has been used to replace human serum albumin (HSA), as these two compounds share a similar structure. Naringin palmitate is a modified product of naringin that is produced by an acylation reaction with palmitic acid, which is considered to be an effective substance for enhancing naringin lipophilicity. In this study, the interaction of naringin palmitate with BSA was c...

  2. Lipid-rich bovine serum albumin improves the viability and hatching ability of porcine blastocysts produced in vitro

    OpenAIRE

    Suzuki, Chie; SAKAGUCHI, Yosuke; Hoshi, Hiroyoshi; Yoshioka, Koji

    2015-01-01

    The effects of lipid-rich bovine serum albumin (LR-BSA) on the development of porcine blastocysts produced in vitro were examined. Addition of 0.5 to 5 mg/ml LR-BSA to porcine blastocyst medium (PBM) from Day 5 (Day 0 = in vitro fertilization) significantly increased the hatching rates of blastocysts on Day 7 and the total cell numbers in Day-7 blastocysts. When Day-5 blastocysts were cultured with PBM alone, PBM containing LR-BSA, recombinant human serum albumin or fatty acid-free BSA, addit...

  3. Silver nanoclusters emitting weak NIR fluorescence biomineralized by BSA

    Science.gov (United States)

    Li, Baoshun; Li, Jianjun; Zhao, Junwu

    2015-01-01

    Noble metal (e.g., gold and silver) nanomaterials possess unique physical and chemical properties. In present work, silver nanoclusters (also known as silver quantum clusters or silver quantum dots) were synthesized by bovine serum albumin (BSA) biomineralization. The synthesized silver nanoclusters were characterized by UV-VIS absorption spectroscopy, fluorescence spectroscopy, upconversion emission spectroscopy, TEM, HRTEM and FTIR spectroscopy. TEM results showed that the average size of the silver nanoclusters was 2.23 nm. Fluorescence results showed that these silver nanoclusters could emit weak near-infrared (NIR) fluorescence (the central emission wavelength being about 765 nm). And the central excitation wavelength was about 395 nm, in the UV spectral region. These silver nanoclusters showed an extraordinarily large gap (about 370 nm) between the central excitation wavelength and central emission wavelength. In addition, it was found that these silver nanoclusters possess upconversion emission property. Upconversion emission results showed that the upconversion emission spectrum of the silver nanoclusters agreed well with their normal fluorescence emission spectrum. The synthesized silver nanoclusters showed high stability in aqueous solution and it was considered that they might be confined in BSA molecules. It was found that silver nanoclusters might enhance and broaden the absorption of proteins, and the protein absorption peak showed an obvious red shift (being 7 nm) after the formation of silver nanoclusters.

  4. Direct determination of naturally occurring biologically active compound–serum albumin conjugate by matrix-assisted laser desorption/ionization mass spectrometry

    OpenAIRE

    Tanaka, H.; Xuan, L.J.; S. Morimoto; Shoyama, Y.; Isobe, R.; Nojima, K.

    2001-01-01

    Opium alkaloids were conjugated with bovine serum albumin (BSA) to give individual antigen conjugates which were analyzed using BSA as an internal standard by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. It became clear that 9 molecules of thebaine were conjugated in a thebaine–BSA conjugate. Codeine and morphine contents in individual conjugates were determined to be 12 and 6 molecules, respectively. Using a relative molecular mass of BSA, 11.5 molecules of forskoli...

  5. Spectroscopic investigation of the interaction between riboflavin and bovine serum albumin

    Science.gov (United States)

    Guo, Xing-Jia; Sun, Xiu-Dan; Xu, Shu-Kun

    2009-08-01

    The mutual interaction of riboflavin (RF) with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy under simulative physiological conditions. The fluorescence quenching mechanism of BSA by RF should belong to dynamic quenching according to the Stern-Volmer equation, but also the effect of ground complex formation and energy transfer could not be completely precluded in BSA-RF system. The binding constants and the corresponding thermodynamic parameters at different temperatures were calculated, which indicated the presence of hydrophobic forces between RF and BSA. The averaged binding distance between riboflavin and BSA was also obtained based on the theory of FÖrster's non-radiation energy transfer. Moreover, the effect of riboflavin on the conformation of BSA was analyzed using synchronous fluorescence. The effects of some common ions Cu 2+, Zn 2+, Ca 2+, and Mg 2+ on the binding constant between riboflavin and BSA were also examined.

  6. Conversion of 2'-substituted chalcones in the presence of BSA as evidenced by (1)H NMR studies.

    Science.gov (United States)

    Raghav, Neera; Garg, Shweta; Ravish, Indu

    2016-04-01

    The emergence of albumin as a biocatalyst has created continuous interest of researchers for its application not only in the field of asymmetric oxidations and reductions but also in chemical reactions such as additions, condensations and eliminations. In the present work we report the cyclization reactions in presence of an albumin protein, Bovine Serum Albumin (BSA). The work is focused on cyclization of 2'-hydroxychalcone and 2'-aminochalcone to flavanones and azaflavanone, respectively. The results are supported by (1)H NMR studies. PMID:26723247

  7. Rotational diffusion of bovine serum albumin denaturated by sodium dodecylsulfate, According to data from tryptophan fluorescence

    Science.gov (United States)

    Vlasova, I. M.; Zhuravleva, V. V.; Saletskii, A. M.

    2014-03-01

    The rotational diffusion of bovine serum albumin (BSA) molecules in solutions with different concentrations of the anionic detergent sodium dodecylsulfate (SDS) at different pH values is investigated, yielding information on the denaturation of BSA under the action of SDS. It is found from the increased degree of polarization in the tryptophan fluorescence of BSA and the registered parameters for the rotational diffusion of BSA molecules that the denaturation of BSA under the action of SDS at pH values less than the isoelectric point (pI) of BSA (4-9) is a two-stage process. It is shown that the first stage of BSA denaturation common for all pH values is the decondensation of BSA globules, while the second stage of BSA denaturation at pH greater than the pI of BSA is the unfolding of the protein's amino acid chain. It is concluded that the denaturation of BSA under the action of SDS proceeds more deeply at pH values greater than the pI of BSA.

  8. Structural influence of graft and block polycations on the adsorption of BSA.

    Science.gov (United States)

    Zhang, Li; Jin, Fengmin; Zhang, Tingbin; Zhang, Ling; Xing, Jinfeng

    2016-04-01

    Protein adsorption is considered as an important factor for the low transfection efficiency of polycations in vivo. In this study, two typical polycations of equal molecular weight with different structures were chosen to investigate their adsorption on bovine serum albumin (BSA), including the block copolymer named poly (N-vinylpyrrolidone)-b-poly (2-dimethylaminoethyl methacrylate) (PVP-b-PDMAEMA, i.e. PbP) and graft copolymer named PVP-g-PDMAEMA (PgP), respectively. Fluorescence spectroscopy was used to confirm the binding constants and binding sites between polycations and BSA in static state. The binding constants were 4.1×10(4)M(-1) vs 8.3×10(4)M(-1) and binding sites were 0.3 vs 1.1 for PbP and PgP, respectively, indicating PgP had stronger binding affinity with BSA. Surface plasmon resonance (SPR) was used to study the dynamical non-specific interaction between BSA and polycations as well as the polyplexes. The numbers of both PbP and PgP adsorbed on BSA increased with concentration of polycations increasing, and the number of PgP adsorbed on BSA is higher compared with PbP when their concentration is low. When their concentration is high, the number of PbP adsorbed on BSA is more than that of PgP. However, PgP/DNA polyplexes showed higher adsorption amount compared with PbP/DNA polyplexes at different N/P ratios. PMID:26763174

  9. Drug Delivery Vehicles Based on Albumin-Polymer Conjugates.

    Science.gov (United States)

    Jiang, Yanyan; Stenzel, Martina

    2016-06-01

    Albumin has been a popular building block to create nanoparticles for drug delivery purposes. The performance of albumin as a drug carrier can be enhanced by combining protein with polymers, which allows the design of carriers to encompass a broader spectrum of drugs while features unique to synthetic polymers such as stimuli-responsiveness are introduced. Nanoparticles based on polymer-albumin hybrids can be divided into two classes: one that carries album as a bioactive surface coating and the other that uses albumin as biocompatible, although nonbioactive, building block. Nanoparticles with bioactive albumin surface coating can either be prepared by self-assembly of albumin-polymer conjugates or by postcoating of existing nanoparticles with albumin. Albumin has also been used as building block, either in its native or denatured form. Existing albumin nanoparticles are coated with polymers, which can influence the degradation of albumin or impact on the drug release. Finally, an alternative way of using albumin by denaturing the protein to generate a highly functional chain, which can be modified with polymer, has been presented. These albumin nanoparticles are designed to be extremely versatile so that they can deliver a wide variety of drugs, including traditional hydrophobic drugs, metal-based drugs and even therapeutic proteins and siRNA. PMID:26947019

  10. Photodynamically generated bovine serum albumin radicals

    DEFF Research Database (Denmark)

    Silvester, J A; Timmins, G S; Davies, Michael Jonathan

    1998-01-01

    Porphyrin-sensitized photoxidation of bovine serum albumin (BSA) results in oxidation of the protein at (at least) two different, specific sites: the Cys-34 residue giving rise to a thiyl radical (RS.); and one or both of the tryptophan residues (Trp-134 and Trp-214) resulting in the formation of...... by a range of proteases. The generation of protein-derived radicals also results in an enhancement of photobleaching of the porphyrin, suggesting that protein radical generation is linked to porphyrin photooxidation....

  11. Synthesis of 5-Fluorouracil conjugated LaF{sub 3}:Tb{sup 3+}/PEG-COOH nanoparticles and its studies on the interaction with bovine serum albumin: spectroscopic approach

    Energy Technology Data Exchange (ETDEWEB)

    Mangaiyarkarasi, Rajendiran; Chinnathambi, Shanmugavel; Aruna, Prakasarao; Ganesan, Singaravelu, E-mail: sganesan@annauniv.edu, E-mail: ganesansingaravelu@gmail.com [Anna University, Department of Medical Physics (India)

    2015-03-15

    The luminescent lanthanide-doped nanoparticles have gathered considerable attention in many fields especially in biomedicine. In this work, the lanthanum fluoride-doped terbium nanoparticles (LaF{sub 3}:Tb{sup 3+} NPs) via simple chemical precipitation method has been synthesized and functionalized with polyethylene glycol. The size and the shape of the nanoparticles are confirmed using X-ray diffraction and transmission electron microscopy. The conjugation of 5-Fluorouracil (5-FU) and thus synthesized nanoparticles (NPs) were confirmed using various spectroscopic methods such as UV–Visible spectroscopy, fluorescence steady state, and excited state spectroscopy studies. The enhancement in fluorescence emission (λ = 543 nm) of drug-conjugated nanoparticles confirms the Vander Waals force of attraction due to F–F bonding between the drug and the nanoparticles. Further, the effects of 5FU-NPs in carrier protein were investigated using bovine serum albumin as a protein model. The 5FU–LaF{sub 3}:Tb{sup 3+} nanoparticles binding is illustrated with binding constant and number of binding sites. The structural change of bovine serum albumin has been studied using circular dichroism and Fourier transform infrared spectroscopy analysis.

  12. Photophysical investigations of squaraine and cyanine dyes and their interaction with bovine serum albumin

    Science.gov (United States)

    Saikiran, M.; Sato, D.; Pandey, S. S.; Kato, T.

    2016-04-01

    A model far-red sensitive symmetrical squaraine dye (SQ-3) and unsymmetrical near infra-red sensitive cyanine dye (UCD-1) bearing direct–COOH functionalized indole ring were synthesized, characterized and subjected to photophysical investigations including their interaction with bovine serum albumin (BSA) as a model protein in phosphate buffer solution (PBS). Both of the dyes exhibit strong interaction with BSA in phosphate buffer with high apparent binding constant. A judicious tuning of hydrophobic main backbone with reactive functionality for associative interaction with active site of BSA has been found to be necessary for BSA detection in PBS.

  13. Albumin Supplement Affects the Metabolism and Metabolism-Related Drug-Drug Interaction of Fenoprofen Enantiomers.

    Science.gov (United States)

    Wang, Nan; Wang, Feng; Meng, Yu; Yang, Guo-Hui; Chen, Ju-Wu; Wang, Jia-Xiang

    2015-07-01

    The influence of albumin towards the metabolism behavior of fenoprofen enantiomers and relevant drug-drug interaction was investigated in the present study. The metabolic behavior of fenoprofen enantiomers was compared in a phase II metabolic incubation system with and without bovine serum albumin (BSA). BSA supplement increased the binding affinity parameter (Km) of (R)-fenoprofen towards human liver microsomes (HLMs) from 148.3 to 214.4 μM. In contrast, BSA supplement decreased the Km of (S)-fenoprofen towards HLMs from 218.2 to 123.5 μM. For maximum reaction velocity (Vmax), the addition of BSA increased the Vmax of (R)-fenoprofen from 1.3 to 1.6 nmol/min/mg protein. In the contrast, BSA supplement decreased the Vmax value from 3.3 to 1.5 nmol/min/mg protein. Andrographolide-fenoprofen interaction was used as an example to investigate the influence of BSA supplement towards fenoprofen-relevant drug-drug interaction. The addition of 0.2% BSA in the incubation system significantly decreased the inhibition potential of andrographolide towards (R)-fenoprofen metabolism (P andrographolide towards the metabolism of (S)-fenoprofen. BSA supplement also changed the inhibition kinetic type and parameter of andrographolide towards the metabolism of (S)-fenoprofen. In conclusion, albumin supplement changes the metabolic behavior of fenoprofen enantiomers and the fenoprofen-andrographolide interaction. PMID:26037509

  14. Synthesis and Characterization of Bovine Serum Albumin-Conjugated Copper Sulfide Nanocomposites

    Directory of Open Access Journals (Sweden)

    Peng Huang

    2010-01-01

    Full Text Available A simple biomolecule-assisted solution route was developed to synthesize Bovine Serum Albumin-conjugated copper sulfide (CuS/BSA nanocomposites, directly using copper salts and thioacetamide (TAA as the starting materials with a zwitterionic surfactant Bovine Serum Albumin (BSA as foaming and stabilizing agent. The CuS/BSA nanocomposites have been characterized by UV, TEM, Zeta, DLS, XRD, and FTIR. The results indicate that the as-prepared CuS/BSA nanocomposites are approximate sphere with a size distribution from 10 to 35 nm in diameter and good dispersibility, depending highly on concentration of BSA concentration. These protein-assisted synthesized nanocomposites have a great potential application in biomedical engineering and microelectronics.

  15. Nitidine chloride-assisted bio-functionalization of reduced graphene oxide by bovine serum albumin for impedimetric immunosensing.

    Science.gov (United States)

    Li, Yu; Zhang, Zhao; Zhang, Yuting; Deng, Dongmei; Luo, Liqiang; Han, Baosan; Fan, Chunhai

    2016-05-15

    A novel protocol of label-free electrochemical impedance immunosensor based on bovine serum albumin-nitidine chloride-reduced graphene oxide (BSA-NC-rGO) nanocomposite was proposed for quantitative determination of carcino-embryonic antigen (CEA). BSA was anchored to rGO via the aromatic plane of NC by π-stacking interaction to realize bio-functionalization of rGO, and then gold nanoparticles (AuNPs) were electrodeposited onto the surface of BSA-NC-rGO nanocomposite. The morphology, conductivity and interaction of different nanocomposites were characterized by scanning electron microscopy, cyclic voltammetry, electrochemical impedance spectroscopy (EIS) and UV-vis spectrum. CEA monoclonal antibody (anti-CEA) was conjugated to AuNPs via gold-thiol chemistry to construct electrochemical immunosensing platform, and the specific immunoreaction between CEA and anti-CEA was monitored by EIS. Under optimum conditions, CEA could be quantified in a wide range of 0.1-200ngmL(-1) (R=0.9948) with low detection limit of 0.067ngmL(-1). The proposed immunosensor exhibited great potential for detecting blood samples. PMID:26748371

  16. Spectroscopic Investigation on the Interaction of a Cyanine Dye with Serum Albumins

    Institute of Scientific and Technical Information of China (English)

    ZHANG Ya-Zhou; YANG Qian-Fan; DU Hong-Yan; TANG Ya-Lin; XU Guang-Zhi; YAN Wen-Peng

    2008-01-01

    The interactions of a cyanine dye with human serum albumin (HSA) and bovine serum albumin (BSA) have been investigated by using absorption and fluorescence spectra.Absorption spectral studies show that binding to the serum albumins leads to a bathochromic shift of the monomer band together with a notable intensity change.Furthermore, the number of binding sites (n) was identified by the absorption spectra.There is a constant enhancement of fluorescence quantum yield when the cyanine dye complexes with HSA or BSA.The apparent binding constant (Ka) and the free energy changes (△G) were obtained by analysis of fluorescence data of the cyanine dye in the absence and presence of HSA and BSA.Compared to BSA, HSA associates with the dye in a stronger way.

  17. Application of a fluorescent biosensor based-on magneto-γ-Fe2 O3 -methyldopa nanoparticles for adsorption of human serum albumin.

    Science.gov (United States)

    Shahabadi, Nahid; Maghsudi, Maryam; Shiri, Farshad

    2016-06-01

    Understanding and controlling the interaction between the polymer methyldopa (2-amino-3-(3,4-dihydroxyphenyl)-2-methyl-propanoic acid) (PMDP)-γ-Fe2 O3 nanoparticles and biological fluids is important if the potential of nanoparticles (NPs) in biomedicine is to be realized. Physicochemical studies on the interactions between proteins and NPs are influenced by the surface properties of the NPs. To identify the effects of the NP surface, interactions between human serum albumin (HSA) and PMDP-γ-Fe2 O3 NPs were investigated. Here, the adsorption of HSA onto small (10-30 nm diameter) PMDP-γ-Fe2 O3 NPs was quantitatively analyzed using spectroscopic methods. The fluorescence quenching data were checked for the inner-filter effect, the main confounding factor in the observed quenching. The binding constants, Ka , were calculated at different temperatures, using a nonlinear fit to the experimental data, and the thermodynamic parameters ∆H, ∆S and ∆G were given. The obtained thermodynamic signature suggests that hydrophobic interactions at least are present. This result indicates that the structure of the protein turns from a structureless denatured state at pH 3 into an ordered biologically active native state on addition of PMDP-γ-Fe2 O3 NPs. Copyright © 2015 John Wiley & Sons, Ltd. PMID:26542088

  18. Albumin-NIR dye self-assembled nanoparticles for photoacoustic pH imaging and pH-responsive photothermal therapy effective for large tumors.

    Science.gov (United States)

    Chen, Qian; Liu, Xiaodong; Zeng, Jianfeng; Cheng, Zhenping; Liu, Zhuang

    2016-08-01

    Real-time in vivo pH imaging in the tumor, as well as designing therapies responsive to the acidic tumor microenvironment to achieve optimized therapeutic outcomes have been of great interests in the field of nanomedicine. Herein, a pH-responsive near-infrared (NIR) croconine (Croc) dye is able to induce the self-assembly of human serum albumin (HSA) to form HSA-Croc nanoparticles useful not only for real-time ratiometric photoacoustic pH imaging of the tumor, but also for pH responsive photothermal therapy with unexpected great performance against tumors with relatively large sizes. Such HSA-Croc nanoparticles upon intravenous injection exhibit efficient tumor homing. As the decrease of pH, the absorption of Croc at 810 nm would increase while that at 680 nm would decrease, allowing real-time pH sensing in the tumor by double-wavelength ratiometric photoacoustic imaging, which reveals the largely decreased pH inside the cores of large tumors. Moreover, utilizing HSA-Croc as a pH-responsive photothermal agent, effective photothermal ablation of large tumors is realized, likely owing to the more evenly distributed intratumoral heating compared to that achieved by conventional pH-insensitive photothermal agents, which are effective mostly for tumors with small sizes. PMID:27177219

  19. BSA 500 UOP Course Tutorial/TutotorialRank

    OpenAIRE

    ruomz

    2015-01-01

    For more course tutorials visit www.tutorialrank.com Tutorial Purchased: 4 Times, Rating: A+ BSA 500 Week 1 Learning Team Charter (UOP Course) BSA 500 Week 2 Individual Assignment Virtual Organizations Table Part I (UOP Course) BSA 500 Week 3 Individual Assignment Table 1 Part 2 Virtual Organization (UOP Course) BSA 500 Week 4 Individual Assingment Balance Sheet and Income Statement (UOP Course) BSA 500 Week 5 Individual Assignment Financial Ratios Analysis (Riorda...

  20. Study on the Interaction between CdSe Quantum Dots and Bovine Serum Albumin with Ultraviolet Visible Absorption Spectroscopy

    Institute of Scientific and Technical Information of China (English)

    He You HAN; De Hong HU; Jian Gong LIANG; Zong Hai SHENG

    2006-01-01

    The interaction of CdSe quantum dots (QDs) with bovine serum albumin (BSA) has been investigated with ultraviolet visible absorption spectroscopy (UVAS). It was found that the absorption intensity of CdSe QDs significantly decreased after adding BSA solution, showing that CdSe QDs were bonded to BSA. The binding molar ratio was 1:1 and the binding constant was 9.7 × 106 L mol-1.

  1. Binding of the neuroleptic drug, gabapentin, to bovine serum albumin: Insights from experimental and computational studies

    International Nuclear Information System (INIS)

    The interaction between antiepileptic drug, gabapentin (GP), and bovin serum albumin (BSA) was studied by spectroscopic and computational methods. The native fluorescence of BSA was quenched by GP. Stern–Volmer quenching constant was calculated at different temperatures which suggested a static mechanism. The association constant (Ka) was calculated from fluorescence quenching studies, which increased with temperature rising. GP competed well with warfarine for hydrophobic subdomain IIA (Sudlow's site I) on the protein. Enthalpy and entropy changes during the interaction of GP with BSA were obtained using van't Hoff plot, which showed an entropy-driven process and involvement of hydrophobic forces (ΔH>0 and ΔS>0). Synchronous fluorescence measurements of BSA solution in the presence of GP showed a considerable blue shift when Δλ=15 nm, therefore, GP interacts with tyrosine-rich sites on BSA. Optimized docked model of BSA–GP mixture confirmed the experimental results. -- Highlights: • Interaction of gabapentin and bovine serum albumin (BSA) is investigated by spectroscopic techniques. • Gabapentin can quench the fluorescence of BSA through a static quenching procedure. • The binding of gabapentin to BSA is driven mainly by hydrophobic interactions. • Subdomain IIA (Sudlow's site I) of BSA is found to be the main binding site for gabapentin. • Molecular docking modeling confirmed the experimental results

  2. Receptor-mediated Hepatic Uptake of M6P-BSA-conjugated Triplex Forming Oligonucleotides in Rats†

    OpenAIRE

    Ye, Zhaoyang; Cheng, Kun; Guntaka, Ramareddy V.; Mahato, Ram I.

    2006-01-01

    Excessive production of extracellular matrix, predominantly type I collagen results in liver fibrosis. Earlier we synthesized mannose 6-phosphate-bovine serum albumin (M6P-BSA) and conjugated to the type I collagen specific triplex forming oligonucleotide (TFO) for its enhanced delivery to hepatic stellate cells (HSCs), which is the principle liver fibrogenic cell. In this report, we demonstrate a time-dependent cellular uptake of M6P-BSA-33P-TFO by HSC-T6 cells. Both cellular uptake and nucl...

  3. Evaluation of BSA protein release from hollow hydroxyapatite microspheres into PEG hydrogel

    International Nuclear Information System (INIS)

    Implants that simultaneously function as an osteoconductive matrix and as a device for local drug or growth factor delivery could provide an attractive system for bone regeneration. In our previous work, we prepared hollow hydroxyapatite (abbreviated HA) microspheres with a high surface area and mesoporous shell wall and studied the release of a model protein, bovine serum albumin (BSA), from the microspheres into phosphate-buffered saline (PBS). The present work is an extension of our previous work to study the release of BSA from similar HA microspheres into a biocompatible hydrogel, poly(ethylene glycol) (PEG). BSA-loaded HA microspheres were placed in a PEG solution which was rapidly gelled using ultraviolet radiation. The BSA release rate into the PEG hydrogel, measured using a spectrophotometric method, was slower than into PBS, and it was dependent on the initial BSA loading and on the microstructure of the microsphere shell wall. A total of 35–40% of the BSA initially loaded into the microspheres was released into PEG over ∼ 14 days. The results indicate that these hollow HA microspheres have promising potential as an osteoconductive device for local drug or growth factor delivery in bone regeneration and in the treatment of bone diseases. - Highlights: ► Novel multifunctional system, hollow hydroxyapatite (HA) microspheres, was evaluated. ► System can simultaneously provide osteoconductivity and local protein delivery. ► HA microspheres showed sustained release of a protein into an ECM-like medium. ► HA microspheres have promising potential for use in bone regeneration

  4. Interaction of BODIPY dyes with bovine serum albumin: a case study on the aggregation of a click-BODIPY dye.

    Science.gov (United States)

    Jameson, Laramie P; Smith, Nicholas W; Annunziata, Onofrio; Dzyuba, Sergei V

    2016-06-01

    The fluorescence of BODIPY and click-BODIPY dyes was found to substantially increase in the presence of bovine serum albumin (BSA). BSA acted as a solubilizer for dye aggregates, in addition to being a conventional binding scaffold for the click-BODIPY dyes, indicating that disaggregation of fluorophores should be considered when evaluating dye-protein interactions. PMID:27173791

  5. Toxicity of silica nanoparticles and the effect of protein corona

    DEFF Research Database (Denmark)

    Foldbjerg, Rasmus; Jespersen, Lars Vesterby; Wang, Jing;

    2010-01-01

      The cytotoxicity of silica nanoparticles (NPs) was investigated in the human lung cell line, A549. Silica NPs of different sizes (DLS size; 16-42 nm) were used to determine appropriate dose metrics whereas the effect of the NP corona was tested by coating the NPs with bovine serum albumin (BSA......). The NPs were characterized by TEM and DLS as monodisperse and non-aggregated in solution and the NP suspensions were free of metal and endotoxin impurities as tested by ICP-MS and the LAL test. Cellular uptake and binding of the silica NPs was indirectly assessed by flow cytometry side scatter and SEM...... upon silica NP exposure. The silica NP surface area was found to be the best dose metric for predicting cytotoxicity and IL-8 release. Generally, the NPs were only cytotoxic at high concentrations and BSA-coating of the NPs significantly decreased the cytotoxicity and cellular IL-8 secretion. All the...

  6. Competitive binding of phenylbutazone and colchicine to serum albumin in multidrug therapy: A spectroscopic study

    Science.gov (United States)

    Sułkowska, A.; Maciążek-Jurczyk, M.; Bojko, B.; Równicka, J.; Zubik-Skupień, I.; Temba, E.; Pentak, D.; Sułkowski, W. W.

    2008-06-01

    The binding sites for phenylbutazone and colchicine were identified in tertiary structure of bovine and human serum albumin with the use of spectrofluorescence analysis. It was found that phenylbutazone has two binding sites in both sera albumins (HSA and BSA), while colchicine has one binding site in BSA as well as in HSA. The comparison of the quenching effect of BSA and HSA fluorescence by phenylbutazone and colchicine allows us to identify subdomain IIA in protein as the binding site for these two drugs. In this subdomain tryptophan 214 is located. The participation of tyrosyl and tryptophanyl residues of protein was also estimated in the drug-albumin complex. The comparison of quenching of fluorescence of HSA and BSA excited at 280 nm with that at 295 nm allowed us to state that the participation of tyrosyl residues of albumin in the phenylbutazone-serum albumin interaction is significant. The analysis of quenching of fluorescence of BSA in the binary and ternary systems showed that phenylbutazone does not affect the complex formed between colchicine and BSA. Similarly, colchicine has no effect on the Phe-BSA complex. However marked differences were observed for the complex with HSA. On the basis of Ka and KQ values it was concluded that colchicine may probably cause displacement of phenylbutazone from its complex with serum albumin (SA). Static and dynamic quenching for the binary and ternary systems is also discussed. The competition of phenylbutazone and colchicine in binding to serum albumin should be taken into account in the multi-drug therapy.

  7. Protein-mediated autoreduction of gold salts to gold nanoparticles

    Energy Technology Data Exchange (ETDEWEB)

    Basu, Nivedita; Bhattacharya, Resham; Mukherjee, Priyabrata [Department of Biochemistry and Molecular Biology, College of Medicine, Mayo Clinic, Rochester, MN 55905 (United States)], E-mail: Mukherjee.Priyabrata@mayo.edu

    2008-09-01

    Here we report for the first time that proteins can function as unique reducing agents to produce gold nanoparticles from gold salts. We demonstrate that three different proteins, namely, bovine serum albumin (BSA), Rituximab (RIT-an anti-CD20 antibody) and Cetuximab (C225-anti-EGFR antibody), reduce gold salts to gold nanoparticles (GNP). Interestingly, among all the three proteins tested, only BSA can reduce gold salts to gold nanotriangles (GNT). BSA-induced formation of GNT can be controlled by carefully selecting the reaction condition. Heating or using excess of ascorbic acid (AA) as additional reducing agent shifts the reaction towards the formation of GNP with flower-like morphology, whereas slowing down the reaction either by cooling or by adding small amount of AA directs the synthesis towards GNT formation. GNT is formed only at pH 3; higher pHs (pH 7 and pH 10) did not produce any nanoparticles, suggesting the involvement of specific protein conformation in GNT formation. The nanomaterials formed by this method were characterized using UV-visible (UV-vis) spectroscopy and transmission electron microscopy (TEM). This is an important finding that will have uses in various nanotechnological applications, particularly in the green synthesis of novel nanomaterials based on protein structure.

  8. Experimental and theoretical study on the binding of 2-mercaptothiazoline to bovine serum albumin

    International Nuclear Information System (INIS)

    2-Mercaptothiazoline (MTZ) is widely utilized as a brightening and stabilization agent, corrosion inhibitor and antifungal reagent. The residue of MTZ in the environment is potentially hazardous to human health. In this study, the binding mode of MTZ with bovine serum albumin (BSA) was investigated using spectroscopic and molecular docking methods under physiological conditions. MTZ could spontaneously bind with BSA through hydrogen bond and van der Waals interactions with one binding site. The site marker displacement experiments and the molecular docking revealed that MTZ bound into site II (subdomain IIIA) of BSA, which further resulted in some backbone structures and microenvironmental changes of BSA. This work is helpful for understanding the transportation, distribution and toxicity effects of MTZ in blood. - Highlights: • The mechanism was explored by multiple spectroscopic and molecular docking methods. • MTZ can spontaneously bind with BSA at subdomain IIIA (site II). • MTZ can lead to some conformational changes of BSA

  9. Spectrometric studies on the interaction of fluoroquinolones and bovine serum albumin

    Science.gov (United States)

    Ni, Yongnian; Su, Shaojing; Kokot, Serge

    2010-02-01

    The interaction between fluoroquinolones (FQs), ofloxacin and enrofloxacin, and bovine serum albumin (BSA) was investigated by fluorescence and UV-vis spectroscopy. It was demonstrated that the fluorescence quenching of BSA by FQ is a result of the formation of the FQ-BSA complex stabilized, in the main, by hydrogen bonds and van der Waals forces. The Stern-Volmer quenching constant, KSV, and the corresponding thermodynamic parameters, Δ H, Δ S and Δ G, were estimated. The distance, r, between the donor, BSA, and the acceptor, FQ, was estimated from fluorescence resonance energy transfer (FRET). The effect of FQ on the conformation of BSA was analyzed with the aid of UV-vis absorbance spectra and synchronous fluorescence spectroscopy. Spectral analysis showed that the two FQs affected the conformation of the BSA but in a different manner. Thus, with ofloxacin, the polarity around the tryptophan residues decreased and the hydrophobicity increased, while for enrofloxacin, the opposite effect was observed.

  10. Experimental and theoretical study on the binding of 2-mercaptothiazoline to bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Teng, Yue, E-mail: tengyue@jiangnan.edu.cn; Wang, Xiang; Zou, Luyi; Huang, Ming; Du, Xianzheng

    2015-05-15

    2-Mercaptothiazoline (MTZ) is widely utilized as a brightening and stabilization agent, corrosion inhibitor and antifungal reagent. The residue of MTZ in the environment is potentially hazardous to human health. In this study, the binding mode of MTZ with bovine serum albumin (BSA) was investigated using spectroscopic and molecular docking methods under physiological conditions. MTZ could spontaneously bind with BSA through hydrogen bond and van der Waals interactions with one binding site. The site marker displacement experiments and the molecular docking revealed that MTZ bound into site II (subdomain IIIA) of BSA, which further resulted in some backbone structures and microenvironmental changes of BSA. This work is helpful for understanding the transportation, distribution and toxicity effects of MTZ in blood. - Highlights: • The mechanism was explored by multiple spectroscopic and molecular docking methods. • MTZ can spontaneously bind with BSA at subdomain IIIA (site II). • MTZ can lead to some conformational changes of BSA.

  11. The interaction between 4-aminoantipyrine and bovine serum albumin: Multiple spectroscopic and molecular docking investigations

    International Nuclear Information System (INIS)

    4-Aminoantipyrine (AAP) is widely used in the pharmaceutical industry, in biochemical experiments and in environmental monitoring. AAP as an aromatic pollutant in the environment poses a great threat to human health. To evaluate the toxicity of AAP at the protein level, the effects of AAP on bovine serum albumin (BSA) were investigated by multiple spectroscopic techniques and molecular modeling. After the inner filter effect was eliminated, the experimental results showed that AAP effectively quenched the intrinsic fluorescence of BSA via static quenching. The number of binding sites, the binding constant, the thermodynamic parameters and binding subdomain were measured, and indicated that AAP could spontaneously bind with BSA on subdomain IIIA through electrostatic forces. Molecular docking results revealed that AAP interacted with the Glu 488 and Glu 502 residues of BSA. Furthermore, the conformation of BSA was demonstrably changed in the presence of AAP. The skeletal structure of BSA loosened, exposing internal hydrophobic aromatic ring amino acids and peptide strands to the solution.

  12. SDS胶束体系中亚甲蓝与血清白蛋白的相互作用%The Interaction of Methylene Blue and Bovine Serum Albumin in SDS Micelle System

    Institute of Scientific and Technical Information of China (English)

    郭荣; 范国康; 刘天晴; 焦新安

    2001-01-01

    The interaction of methylene blue(MB) and bovine serum albumin(BSA) is investigated in the SDS micelle system which is simulated as one kind of coexisted albumin. The interaction parameters of MB and BSA and simulated albumin such as partition coefficient κ 、 normal binding free energy Δ G 、 average binding number n are calculated. The results show that most of MB is in the form of monomer in SDS micelle systems; the main interaction of MB and BSA is of static electric and H-bind force,and that of MB and simulated albumin is only of static electric force.

  13. Interactions and effects of BSA-functionalized single-walled carbon nanotubes on different cell lines

    Science.gov (United States)

    Muzi, Laura; Tardani, Franco; La Mesa, Camillo; Bonincontro, Adalberto; Bianco, Alberto; Risuleo, Gianfranco

    2016-04-01

    Functionalized carbon nanotubes (CNTs) have shown great promise in several biomedical contexts, spanning from drug delivery to tissue regeneration. Thanks to their unique size-related properties, single-walled CNTs (SWCNTs) are particularly interesting in these fields. However, their use in nanomedicine requires a clear demonstration of their safety in terms of tissue damage, toxicity and pro-inflammatory response. Thus, a better understanding of the cytotoxicity mechanisms, the cellular interactions and the effects that these materials have on cell survival and on biological membranes is an important first step for an appropriate assessment of their biocompatibility. In this study we show how bovine serum albumin (BSA) is able to generate homogeneous and stable dispersions of SWCNTs (BSA-CNTs), suggesting their possible use in the biomedical field. On the other hand, this study wishes to shed more light on the impact and the interactions of protein-stabilized SWCNTs with two different cell types exploiting multidisciplinary techniques. We show that BSA-CNTs are efficiently taken up by cells. We also attempt to describe the effect that the interaction with cells has on the dielectric characteristics of the plasma membrane and ion flux using electrorotation. We then focus on the BSA-CNTs’ acute toxicity using different cellular models. The novel aspect of this work is the evaluation of the membrane alterations that have been poorly investigated to date.

  14. Analytical quality-by-design approach for sample treatment of BSA-containing solutions

    Directory of Open Access Journals (Sweden)

    Lien Taevernier

    2015-02-01

    Full Text Available The sample preparation of samples containing bovine serum albumin (BSA, e.g., as used in transdermal Franz diffusion cell (FDC solutions, was evaluated using an analytical quality-by-design (QbD approach. Traditional precipitation of BSA by adding an equal volume of organic solvent, often successfully used with conventional HPLC-PDA, was found insufficiently robust when novel fused-core HPLC and/or UPLC-MS methods were used. In this study, three factors (acetonitrile (%, formic acid (% and boiling time (min were included in the experimental design to determine an optimal and more suitable sample treatment of BSA-containing FDC solutions. Using a QbD and Derringer desirability (D approach, combining BSA loss, dilution factor and variability, we constructed an optimal working space with the edge of failure defined as D<0.9. The design space is modelled and is confirmed to have an ACN range of 83±3% and FA content of 1±0.25%.

  15. Unfolding and Refolding of Bovine Serum Albumin at Acid pH: Ultrasound and Structural Studies

    OpenAIRE

    El Kadi, N.; Taulier, N.; Le Huérou, J. Y.; Gindre, M.; Urbach, W.; Nwigwe, I.; Kahn, P. C.; Waks, M

    2006-01-01

    Serum albumin is the most abundant protein in the circulatory system. The ability of albumins to undergo a reversible conformational transition, observed with changes in pH, is conserved in distantly related species, suggesting for it a major physiological role possibly related to the transport of small molecules including drugs. We have followed changes of bovine serum albumin (BSA) in volume by densimetry and in adiabatic compressibility during its conformational transition from pH 7–2, usi...

  16. Interactions between U(VI) and bovine serum albumin

    International Nuclear Information System (INIS)

    Interest in bio-toxicology of uranium resulting from its radioactive heavy metal property has been growing enormously in recent years. The interactions between uranium(VI) [U(VI)] and bovine serum albumin (BSA) at physiological pH were studied by spectroscopic methods. Fluorescence results revealed the formation of BSA-U(VI) complex, the binding constants as well as the number of binding sites were determined. In particular, the effects of U(VI) binding on the secondary structures of BSA were examined by means of Fourier transformation infrared spectroscopy equipped with attenuated total reflection (FT-IR/ATR). It was found that the α-helix component of BSA decreased gradually with increasing concentration of U(VI). In contrast, the β-sheets, turns, and random coil structures all increased correspondingly. Our work would shed light on the possible interaction mechanism between U(VI) and proteins in aqueous solutions. (author)

  17. BSA adsorption on bimodal PEO brushes

    NARCIS (Netherlands)

    Bosker, W.T.E.; Iakovlev, P.A.; Norde, W.; Cohen Stuart, M.A.

    2005-01-01

    BSA adsorption onto bimodal PEO brushes at a solid surface was measured using optical reflectometry. Bimodal brushes consist of long (N=770) and short (N=48) PEO chains and were prepared on PS surfaces, applying mixtures of PS 29-PEO48 and PS37-PEO770 block copolymers and using the Langmuir-Blodgett

  18. BSA adsorption on bimodal PEO brushes

    NARCIS (Netherlands)

    Bosker, WTE; Iakovlev, PA; Norde, W; Stuart, MAC

    2005-01-01

    BSA adsorption onto bimodal PEO brushes at a solid surface was measured using optical reflectometry. Bimodal brushes consist of long (N = 770) and short (N = 48) PEO chains and were prepared on PS surfaces, applying mixtures of PS29-PEO48 and PS37-PEO770 block copolymers and using the Langmuir-Blodg

  19. Towards hybrid biocompatible magnetic rHuman serum albumin-based nanoparticles: use of ultra-small (CeLn)3/4+ cation-doped maghemite nanoparticles as functional shell

    International Nuclear Information System (INIS)

    Human serum albumin (HSA) is a protein found in human blood. Over the last decade, HSA has been evaluated as a promising drug carrier. However, not being magnetic, HSA cannot be used for biomedical applications such as magnetic resonance imaging (MRI) and magnetic drug targeting. Therefore, subsequent composites building on iron oxide nanoparticles that are already used clinically as MRI contrast agents are extensively studied. Recently and in this context, innovative fully hydrophilic ultra-small CAN-stabilized maghemite ((CeLn)3/4+-γ-Fe2O3) nanoparticles have been readily fabricated. The present study discusses the design, fabrication, and characterization of a dual phase hybrid core (rHSA)-shell ((CeLn)3/4+-γ-Fe2O3 NPs) nanosystem. Quite importantly and in contrast to widely used encapsulation strategies, rHSA NP surface-attached (CeLn)3/4+-γ-Fe2O3 NPs enabled to exploit both rHSA (protein functionalities) and (CeLn)3/4+-γ-Fe2O3 NP surface functionalities (COOH and ligand L coordinative exchange) in addition to very effective MRI contrast capability due to optimal accessibility of H2O molecules with the outer magnetic phase. Resulting hybrid nanoparticles might be used as a platform modular system for therapeutic (drug delivery system) and MR diagnostic purposes. (paper)

  20. Towards hybrid biocompatible magnetic rHuman serum albumin-based nanoparticles: use of ultra-small (CeLn)3/4+ cation-doped maghemite nanoparticles as functional shell

    Science.gov (United States)

    Israel, Liron L.; Kovalenko, Elena I.; Boyko, Anna A.; Sapozhnikov, Alexander M.; Rosenberger, Ina; Kreuter, Jörg; Passoni, Lorena; Lellouche, Jean-Paul

    2015-01-01

    Human serum albumin (HSA) is a protein found in human blood. Over the last decade, HSA has been evaluated as a promising drug carrier. However, not being magnetic, HSA cannot be used for biomedical applications such as magnetic resonance imaging (MRI) and magnetic drug targeting. Therefore, subsequent composites building on iron oxide nanoparticles that are already used clinically as MRI contrast agents are extensively studied. Recently and in this context, innovative fully hydrophilic ultra-small CAN-stabilized maghemite ((CeLn)3/4+-γ-Fe2O3) nanoparticles have been readily fabricated. The present study discusses the design, fabrication, and characterization of a dual phase hybrid core (rHSA)-shell ((CeLn)3/4+-γ-Fe2O3 NPs) nanosystem. Quite importantly and in contrast to widely used encapsulation strategies, rHSA NP surface-attached (CeLn)3/4+-γ-Fe2O3 NPs enabled to exploit both rHSA (protein functionalities) and (CeLn)3/4+-γ-Fe2O3 NP surface functionalities (COOH and ligand L coordinative exchange) in addition to very effective MRI contrast capability due to optimal accessibility of H2O molecules with the outer magnetic phase. Resulting hybrid nanoparticles might be used as a platform modular system for therapeutic (drug delivery system) and MR diagnostic purposes.

  1. Investigation of the photocatalytic effect of zinc oxide nanoparticles in the presence of nitrite

    International Nuclear Information System (INIS)

    Highlights: ► Nitrite enhanced the photo-damage by ZnO nanoparticles to BSA and HaCaT cells. ► Protein nitration was induced by nitrite in photo-damaged BSA and HaCaT cells. ► The effects of photo-damage on BSA were affected by various factors. ► 50-nm ZnO induced more apoptosis than 90-nm ZnO in HaCaT cells. -- Abstract: Zinc oxide nanoparticles are widely used in sunscreen products because of their chemical stability and capability of blocking harmful ultraviolet rays. However, zinc oxide nanoparticles can also generate reactive species under ultraviolet irradiation. Because nitrite can form reactive nitrogen species under oxidative stress and because it exists in perspiration and cosmetics, we studied the effects of nitrites on the photocatalytic damage of zinc oxide nanoparticles (50 nm and 90 nm) to bovine serum albumin and human keratinocyte cells under ultraviolet irradiation (365 nm and 254 nm). The results indicate that nitrite plays an enhancing role in photocatalytic damage by breaking amino acid residues and promoting protein oxidation and nitration. The concentrations of zinc oxide and nitrite, the irradiation light and duration, and the pH of the medium are important factors influencing this photocatalytic damage. Size effects of ZnO nanoparticles on bovine serum albumin and keratinocyte cells are different. It is speculated that the extent of photo-damage is partially dependent on the aggregation of zinc oxide. These findings may be valuable for understanding potential risks of applying zinc oxide nanoparticle-containing sunscreens to human skin under sunlight exposure

  2. Investigation of the photocatalytic effect of zinc oxide nanoparticles in the presence of nitrite

    Energy Technology Data Exchange (ETDEWEB)

    Tu, Min; Abbood, Hayder A. [School of Chemistry and Chemical Engineering, Huazhong University of Science and Technology, 1037 Luoyu Road, Wuhan 430074 (China); Institute of Inorganic Chemistry and Chemical Biology, Hubei key Laboratory of Bioinorganic Chemistry and Medicine, 1037 Luoyu Road, Wuhan 430074 (China); Zhu, Zhening [National Center for Nanoscience and Technology, No.11 ZhongGuanCun BeiYiTiao Road, Beijing 100190 (China); Li, Hailing [School of Chemistry and Chemical Engineering, Huazhong University of Science and Technology, 1037 Luoyu Road, Wuhan 430074 (China); Institute of Inorganic Chemistry and Chemical Biology, Hubei key Laboratory of Bioinorganic Chemistry and Medicine, 1037 Luoyu Road, Wuhan 430074 (China); Gao, Zhonghong, E-mail: zhgao144@mail.hust.edu.cn [School of Chemistry and Chemical Engineering, Huazhong University of Science and Technology, 1037 Luoyu Road, Wuhan 430074 (China); Institute of Inorganic Chemistry and Chemical Biology, Hubei key Laboratory of Bioinorganic Chemistry and Medicine, 1037 Luoyu Road, Wuhan 430074 (China)

    2013-01-15

    Highlights: ► Nitrite enhanced the photo-damage by ZnO nanoparticles to BSA and HaCaT cells. ► Protein nitration was induced by nitrite in photo-damaged BSA and HaCaT cells. ► The effects of photo-damage on BSA were affected by various factors. ► 50-nm ZnO induced more apoptosis than 90-nm ZnO in HaCaT cells. -- Abstract: Zinc oxide nanoparticles are widely used in sunscreen products because of their chemical stability and capability of blocking harmful ultraviolet rays. However, zinc oxide nanoparticles can also generate reactive species under ultraviolet irradiation. Because nitrite can form reactive nitrogen species under oxidative stress and because it exists in perspiration and cosmetics, we studied the effects of nitrites on the photocatalytic damage of zinc oxide nanoparticles (50 nm and 90 nm) to bovine serum albumin and human keratinocyte cells under ultraviolet irradiation (365 nm and 254 nm). The results indicate that nitrite plays an enhancing role in photocatalytic damage by breaking amino acid residues and promoting protein oxidation and nitration. The concentrations of zinc oxide and nitrite, the irradiation light and duration, and the pH of the medium are important factors influencing this photocatalytic damage. Size effects of ZnO nanoparticles on bovine serum albumin and keratinocyte cells are different. It is speculated that the extent of photo-damage is partially dependent on the aggregation of zinc oxide. These findings may be valuable for understanding potential risks of applying zinc oxide nanoparticle-containing sunscreens to human skin under sunlight exposure.

  3. Synthesis, thermodynamic properties and BSA interaction of a new Valen Shiff base derived from o-vanillin and trimethoprim

    International Nuclear Information System (INIS)

    Graphical abstract: A new single Valen Shiff base was synthesized and characterized. The thermodynamics properties of the Shiff base were investigated by microcalorimetry. In particular, the interaction between the synthetic Shiff base and BSA at four different temperatures has been investigated using fluorescence quenching method. - Highlights: • A new single Valen Shiff base was synthesized and characterized. • The thermodynamics properties of the Shiff base were investigated by microcalorimetry. • The interaction between the Shiff base and BSA has been investigated using fluorescence quenching method. - Abstract: A new Valen Shiff base (C22H24N4O5) was synthesized using equivalent moles of o-vanillin and trimethoprim. At 298.15 K, the standard molar enthalpy of formation of the new compound was estimated to be ΔfHmΘ [C22H24N4O5(s), 298.15 K] = −(696.92 ± 1.67) kJ mol−1 by microcalorimetry. In particular, the interaction between the Shiff base and bovine serum albumin (BSA) has been investigated. It was proved that the fluorescence quenching of BSA by Shiff base is a result of the formation of a Shiff base-BSA complex. Quenching constants were determined using the Sterns–Volmer equation to provide a measurement of the binding site between Shiff base and BSA. The thermodynamic parameters ΔG, ΔH, and ΔS of the system at different temperatures were calculated. What is more, the distance r between donor (Trp. 213) and acceptor (Shiff base) was obtained. Finally, synchronous fluorescence spectroscopy data has suggested the association between Shiff base and BSA changed the molecular conformation of BSA

  4. Synthesis, thermodynamic properties and BSA interaction of a new Valen Shiff base derived from o-vanillin and trimethoprim

    Energy Technology Data Exchange (ETDEWEB)

    Li, Xu; Jiang, Jian-Hong; Xiao, Sheng-Xiong [Hunan Provincial Key Laboratory of Xiangnan Rare-Precious Metals Compounds and Applications, Department of Chemistry and Life Science, Xiangnan University, Chenzhou 423000, Hunan Province (China); Gu, Hui-Wen, E-mail: gruyclewee@hnu.edu.cn [State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, Hunan University, Changsha 410082, Hunan Province (China); Li, Chuan-Hua; Ye, Li-Juan; Li, Xia; He, Du-Gui; Yao, Fei-Hong [Hunan Provincial Key Laboratory of Xiangnan Rare-Precious Metals Compounds and Applications, Department of Chemistry and Life Science, Xiangnan University, Chenzhou 423000, Hunan Province (China); Li, Qiang-Guo, E-mail: liqiangguo@163.com [Hunan Provincial Key Laboratory of Xiangnan Rare-Precious Metals Compounds and Applications, Department of Chemistry and Life Science, Xiangnan University, Chenzhou 423000, Hunan Province (China)

    2014-01-10

    Graphical abstract: A new single Valen Shiff base was synthesized and characterized. The thermodynamics properties of the Shiff base were investigated by microcalorimetry. In particular, the interaction between the synthetic Shiff base and BSA at four different temperatures has been investigated using fluorescence quenching method. - Highlights: • A new single Valen Shiff base was synthesized and characterized. • The thermodynamics properties of the Shiff base were investigated by microcalorimetry. • The interaction between the Shiff base and BSA has been investigated using fluorescence quenching method. - Abstract: A new Valen Shiff base (C{sub 22}H{sub 24}N{sub 4}O{sub 5}) was synthesized using equivalent moles of o-vanillin and trimethoprim. At 298.15 K, the standard molar enthalpy of formation of the new compound was estimated to be Δ{sub f}H{sub m}{sup Θ} [C{sub 22}H{sub 24}N{sub 4}O{sub 5}(s), 298.15 K] = −(696.92 ± 1.67) kJ mol{sup −1} by microcalorimetry. In particular, the interaction between the Shiff base and bovine serum albumin (BSA) has been investigated. It was proved that the fluorescence quenching of BSA by Shiff base is a result of the formation of a Shiff base-BSA complex. Quenching constants were determined using the Sterns–Volmer equation to provide a measurement of the binding site between Shiff base and BSA. The thermodynamic parameters ΔG, ΔH, and ΔS of the system at different temperatures were calculated. What is more, the distance r between donor (Trp. 213) and acceptor (Shiff base) was obtained. Finally, synchronous fluorescence spectroscopy data has suggested the association between Shiff base and BSA changed the molecular conformation of BSA.

  5. Influence of binding characteristics of 153Sm-complexes to BSA on their bone uptake

    International Nuclear Information System (INIS)

    The bone uptake in normal mice and adsorption on bone model materials (hydroxyapatite and type I collagen) of 153Sm-NTMP, 153Sm-HEDTMP, 153Sm-DCTMP, 153Sm-EDTMP, 153Sm-DTPMP and 153Sm-DTPA are compared, and then the binding characteristics of these 153Sm-complexes to bovine serum albumin (BSA) are investigated. It is found that there is a discrepancy between the bone uptake and the adsorption on bone model materials, and that the binding characteristics of these 153Sm-complexes to BSA play an important role in the process of their bone uptake. Also, the binding characteristics are applied to explain the discrepancy successfully

  6. The fluorescence spectroscopic studies on the interaction of novel aminophosphinic acids with bovine serum albumin

    International Nuclear Information System (INIS)

    Six novel aminomethylphosphinic acids have been synthesized and characterized. The interaction between the aminophosphinic acids and bovine serum albumin (BSA) was investigated using fluorescence spectroscopy. The experimental results showed that the fluorescence quenching of BSA by aminophosphinic acids is a result of the formation of aminophosphinic acid–BSA complex; static quenching and non-radiative energy transferring were confirmed to result in the fluorescence quenching. The number of binding sites n, the apparent binding constant KA and the corresponding thermodynamic parameters were calculated at different temperatures. The process of binding of the aminophosphinic acid molecules to BSA was a spontaneous molecular interaction procedure in which entropy increased and Gibbs free energy decreased. Hydrophobic interaction force plays a major role in stabilizing the complex. The effect of aminophosphinic acids on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. -- Graphical abstarct: The binding interactions of the water-soluble aminoalkylphosphinic acids APA 1–6 to bovine serum albumin (BSA) showed that the interaction process was spontaneous and the major interaction forces were found to be hydrophobic. Highlights: ► Binding of novel aminophosphinic acids with bovine serum albumin. ► Hydrophobic and hydrogen bonding attraction play major role in the binding process. ► Binding did not cause conformational changes in the protein. ► The quenching mechanism of fluorescence of BSA by aminophosphinic acids is a static quenching process

  7. Effects of Gold Salt Speciation and Structure of Human and Bovine Serum Albumins on the Synthesis and Stability of Gold Nanostructures.

    Science.gov (United States)

    Miranda, Érica G A; Tofanello, Aryane; Brito, Adrianne M M; Lopes, David M; Albuquerque, Lindomar J C; de Castro, Carlos E; Costa, Fanny N; Giacomelli, Fernando C; Ferreira, Fabio F; Araújo-Chaves, Juliana C; Nantes, Iseli L

    2016-01-01

    The present study aimed to investigate the influence of albumin structure and gold speciation on the synthesis of gold nanoparticles (GNPs). The strategy of synthesis was the addition of HAuCl4 solutions at different pH values (3-12) to solutions of human and bovine serum albumins (HSA and BSA) at the same corresponding pH values. Different pH values influence the GNP synthesis due to gold speciation. Besides the inherent effect of pH on the native structure of albumins, the use N-ethylmaleimide (NEM)-treated and heat-denaturated forms of HSA and BSA provided additional insights about the influence of protein structure, net charge, and thiol group approachability on the GNP synthesis. NEM treatment, heating, and the extreme values of pH promoted loss of the native albumin structure. The formation of GNPs indicated by the appearance of surface plasmon resonance (SPR) bands became detectable from 15 days of the synthesis processes that were carried out with native, NEM-treated and heat-denaturated forms of HSA and BSA, exclusively at pH 6 and 7. After 2 months of incubation, SPR band was also detected for all synthesis carried out at pH 8.0. The mean values of the hydrodynamic radius (RH) were 24 and 34 nm for GNPs synthesized with native HSA and BSA, respectively. X-ray diffraction (XRD) revealed crystallites of 13 nm. RH, XRD, and zeta potential values were consistent with GNP capping by the albumins. However, the GNPs produced with NEM-treated and heat-denaturated albumins exhibited loss of protein capping by lowering the ionic strength. This result suggests a significant contribution of non-electrostatic interactions of albumins with the GNP surface, in these conditions. The denaturation of proteins exposes hydrophobic groups to the solvent, and these groups could interact with the gold surface. In these conditions, the thiol blockage or oxidation, the latter probably favored upon heating, impaired the formation of a stable capping by thiol coordination with the

  8. Effects of Gold Salt Speciation and Structure of Human and Bovine Serum Albumins on the Synthesis and Stability of Gold Nanostructures

    Science.gov (United States)

    Miranda, Érica G. A.; Tofanello, Aryane; Brito, Adrianne M. M.; Lopes, David M.; Albuquerque, Lindomar J. C.; de Castro, Carlos E.; Costa, Fanny N.; Giacomelli, Fernando C.; Ferreira, Fabio F.; Araújo-Chaves, Juliana C.; Nantes, Iseli L.

    2016-01-01

    The present study aimed to investigate the influence of albumin structure and gold speciation on the synthesis of gold nanoparticles (GNPs). The strategy of synthesis was the addition of HAuCl4 solutions at different pH values (3–12) to solutions of human and bovine serum albumins (HSA and BSA) at the same corresponding pH values. Different pH values influence the GNP synthesis due to gold speciation. Besides the inherent effect of pH on the native structure of albumins, the use N-ethylmaleimide (NEM)-treated and heat-denaturated forms of HSA and BSA provided additional insights about the influence of protein structure, net charge, and thiol group approachability on the GNP synthesis. NEM treatment, heating, and the extreme values of pH promoted loss of the native albumin structure. The formation of GNPs indicated by the appearance of surface plasmon resonance (SPR) bands became detectable from 15 days of the synthesis processes that were carried out with native, NEM-treated and heat-denaturated forms of HSA and BSA, exclusively at pH 6 and 7. After 2 months of incubation, SPR band was also detected for all synthesis carried out at pH 8.0. The mean values of the hydrodynamic radius (RH) were 24 and 34 nm for GNPs synthesized with native HSA and BSA, respectively. X-ray diffraction (XRD) revealed crystallites of 13 nm. RH, XRD, and zeta potential values were consistent with GNP capping by the albumins. However, the GNPs produced with NEM-treated and heat-denaturated albumins exhibited loss of protein capping by lowering the ionic strength. This result suggests a significant contribution of non-electrostatic interactions of albumins with the GNP surface, in these conditions. The denaturation of proteins exposes hydrophobic groups to the solvent, and these groups could interact with the gold surface. In these conditions, the thiol blockage or oxidation, the latter probably favored upon heating, impaired the formation of a stable capping by thiol coordination with

  9. Dispersion stabilization of silver nanoparticles in synthetic lung fluid studied under in situ conditions

    Energy Technology Data Exchange (ETDEWEB)

    MacCuspie, R.I.; Allen, A.J.; Hackley, V.A. (NIST)

    2014-09-24

    The dispersion stabilization of silver nanoparticles (AgNPs) in synthetic lung fluid was studied to interrogate the effects on colloidal stability due to the principal constituents of the fluid. The colloidal stability of 20 nm citrate-AgNPs dispersed in the presence of each constituent of the synthetic lung fluid (individually, the complete fluid, and without additives) was observed during titration of increasing sodium chloride concentration. A variety of complementary in situ measurement techniques were utilized, including dynamic light scattering, ultraviolet-visible absorption spectroscopy, atomic force microscopy, and small-angle X-ray scattering, which provided a collective set of information that enabled far better understanding of the dispersion behavior in the fluid than any one technique alone. It was observed that AgNPs continued to adsorb bovine serum albumin (BSA) protein from the synthetic lung fluid solution as the sodium chloride concentration increased, until a maximum BSA coating was achieved prior to reaching the physiological sodium chloride concentration of 154 mmol L{sup -1}. BSA was determined to be the constituent of the synthetic lung fluid that is required to provide colloidal stability at high salt loadings, though the phospholipid constituent exerts a subtle effect. Additionally, as AgNPs are a distinctly different class of nanoparticles apart from the carbon nanotubes and titanium dioxide nanoparticles initially reported to be dispersible using this fluid, this work also demonstrates the broad applicability of synthetic lung fluid in providing stable dispersions for engineered nanoparticles for use in biological assays.

  10. Quantification of tannin content in Phyllanthus emblica using radiolabeled BSA by precipitation method

    International Nuclear Information System (INIS)

    Phyllanthus emblica, commonly referred to as 'Indian gooseberry' or 'Amla' is used both as medicine and astonic to build up vitality and vigor. It is one of the constituent of a popular Ayurvedic formulation Triphala churna. Literature shows that there is increasing interest in exploring drugs obtained from plants with a high content of tannins. Tannins, polyphenolic compounds of various molecular weights are found abundantly in nature and have the ability to precipitate proteins. The study aims at quantification of the tannin content of Phyllanthus emblica by radiolabeled Bovine Serum Albumin (BSA) method and to study the antioxidant activity of the crude fruit extract and of the tannin precipitated with BSA from the extract. The fruit was extracted with methanol in the soxhlet apparatus. Precipitation methods like sensitive radiolabeled BSA in which tannins in the plant fruit extract complex with BSA which is quantified by gamma counter along with the reference standards like tannic and gallic acid. Other precipitation method is the radial diffusion assay in which tannin molecules migrate through agarose gel which is impregnated with the protein, BSA. The tannin-protein complex is formed in the gel which appears as a ring. The diameter of the ring is a measure of protein precipitation/binding capacity of tannins. Another method involves precipitation of tannins by polyvinyl poly pyrrolidone (PVPP) and then the total phenol in the supernatant. The difference in the total phenol and that of the supernatant gives the total amount of tannin present in the extract. Antioxidant activity of the crude fruit extract and the tannin present in the extract was assessed by 2,2-diphenyl-1-picrylhydrazyl (DPPH), Hydrogen peroxide scavenging assay. Results show that the total phenol content of the plant was found to be 0.135% in dry matter. The tannin content as shown by the PVPP precipitation method was 12.588 mg while that of Radiolabeled BSA method gave around 10 mg which is

  11. Detection of hepatocellular carcinoma in transgenic mice by Gd-DTPA- and rhodamine 123-conjugated human serum albumin nanoparticles in T1 magnetic resonance imaging.

    Science.gov (United States)

    Watcharin, Waralee; Schmithals, Christian; Pleli, Thomas; Köberle, Verena; Korkusuz, Hüdayi; Hübner, Frank; Waidmann, Oliver; Zeuzem, Stefan; Korf, Horst-Werner; Terfort, Andreas; Gelperina, Svetlana; Vogl, Thomas J; Kreuter, Jörg; Piiper, Albrecht

    2015-02-10

    Nanoparticle (NP)-based contrast agents that enable high resolution anatomic T1-weighted magnetic resonance imaging (MRI) offer the prospect of improving differential diagnosis of liver tumors such as hepatocellular carcinoma (HCC). In the present study, we investigated the possibility of employing novel non-toxic human serum albumin nanoparticles conjugated with Gd-DTPA and rhodamine 123 (Gd-Rho-HSA-NPs) for the detection of HCC by T1-weighted MRI. In addition, the influence of surface coating of the NPs with poloxamine 908, which alters the absorptive behavior of NPs and changes their distribution between the liver and tumor was examined. MRI of transgenic mice with endogenously formed HCCs following intravenous injection of Gd-Rho-HSA-NPs revealed a strong negative contrast of the tumors. Contrasting of the HCCs by NP-enhanced MRI required less Gd as compared to gadolinium-ethoxybenzyl-diethylenetriaminepentaacetic acid-enhanced MRI, which currently provides the most sensitive detection of HCC in patients. Immunohistochemical analyses revealed that the Gd-Rho-HSA-NPs were localized to macrophages, which were - similar to HCC in patients - fewer in number in HCC as compared to the liver tissue, which is in agreement with the negative contrasting of HCC in Gd-Rho-HSA-NP-enhanced MRI. Poloxamine-coated NPs showed lower accumulation in the tumor macrophages and caused a longer lasting enhancement of the MRI signal. These data indicate that Gd-Rho-HSA-NPs enable sensitive detection of HCC by T1-weighted MRI in mice with endogenous HCC through their uptake by macrophages. Poloxamine coating of the NPs delayed the tumor localization of the NPs. PMID:25499552

  12. The labelling of adriamycin-loaded human serum albumin immuno-nanoparticles led by monoclonal antibodies with 131I and its anti-hepatoma effect in vivo

    International Nuclear Information System (INIS)

    The pharmaceutics character, targeting to hepatoma and anticancer activity in nude mice of adriamycin-loaded human serum albumin immuno-nanoparticles (ADR-HSA-NP) against hepatoma led by anti-human hepatoma monoclonal antibodies HAb18 are studied. The results show that effective loaded drug dose of HAb18-ADR-HSA-NP is 1.44%, which is lower than ADR-HSA-NP (1.69%); HAb18-ADR-HSA-NP slowly releases drug ADR and its maximum releasing drug dose (41%) is obviously lower than ADR-HSA-NP (65%) (P 131I-HAb18-ADR-HSA-NP mainly accumulates in liver and its liver-taxis and stability are better than 131I-ADR-HSA-NP in nude mice by intravenous injection; HAb18-ADR-HSA-NP mainly accumulates in tumor and its accumulation amount of tumor is higher than ADR-HSA-NP (P < 0.05), and has obvious inhibiting cancer action and its inhibitory rate of cancer is also higher than ADR-HSA-NP (P < 0.05) by tumor injection. So, HAb18-ADR-HSA-NP can bind and inhibit hepatoma cell from growing in vivo

  13. Albumin coated liposomes: a novel platform for macrophage specific drug delivery

    Directory of Open Access Journals (Sweden)

    Clément Vuarchey

    2011-07-01

    Full Text Available Here we report a new and efficient approach of macrophage specific drug delivery by coating liposomes with albumin. Activated albumin was reacted with liposomes containing polyethylene glycol (PEG as hydrophilic spacers to create a flexible layer of covalently bound albumin molecules on the liposome surface. Albumin coated liposomes were taken up faster and more efficiently than uncoated liposomes by murine macrophages. Liposome uptake was significantly higher in macropha - ges as compared to other cell types tested (endothelial cells, fibroblasts, tumor cells, suggesting specificity for macrophages. In vivo, splenic macrophages phagocytosed BSA coated liposomes (BSA-L at faster rates compared to conventional liposomes (L and PEG liposomes (PEG-L. To prove the effectiveness of this new macrophage specific drug carrier, the bisphosphonates clodronate and zoledronate were encapsulated in BSA-L and compared with conventional liposomes. In vitro, treatment of macrophages with clodronate or zoledronate in BSA-L led to cytotoxic activity within a very short time and to up to 50-fold reduced IC50 concentrations. In vivo, clodronate encapsulated in BSA-L depleted splenic macrophages at a 5-fold lower concentration as conventional clodronate-liposomes. Our results highlight the pharmaceutical benefits of albumin-coated liposomes for macrophage specific drug delivery.

  14. Core-shell-corona doxorubicin-loaded superparamagnetic Fe3O4 nanoparticles for cancer theranostics.

    Science.gov (United States)

    Semkina, A; Abakumov, M; Grinenko, N; Abakumov, A; Skorikov, A; Mironova, E; Davydova, G; Majouga, A G; Nukolova, N; Kabanov, A; Chekhonin, V

    2015-12-01

    Superparamagnetic iron oxide magnetic nanoparticles (MNPs) are successfully used as contrast agents in magnetic-resonance imaging. They can be easily functionalized for drug delivery functions, demonstrating great potential for both imaging and therapeutic applications. Here we developed new pH-responsive theranostic core-shell-corona nanoparticles consisting of superparamagentic Fe3O4 core that displays high T2 relaxivity, bovine serum albumin (BSA) shell that binds anticancer drug, doxorubicin (Dox) and poly(ethylene glycol) (PEG) corona that increases stability and biocompatibility. The nanoparticles were produced by adsorption of the BSA shell onto the Fe3O4 core followed by crosslinking of the protein layer and subsequent grafting of the PEG corona using monoamino-terminated PEG via carbodiimide chemistry. The hydrodynamic diameter, zeta-potential, composition and T2 relaxivity of the resulting nanoparticles were characterized using transmission electron microscopy, dynamic light scattering, thermogravimetric analysis and T2-relaxometry. Nanoparticles were shown to absorb Dox molecules, possibly through a combination of electrostatic and hydrophobic interactions. The loading capacity (LC) of the nanoparticles was 8 wt.%. The Dox loaded nanoparticles release the drug at a higher rate at pH 5.5 compared to pH 7.4 and display similar cytotoxicity against C6 and HEK293 cells as the free Dox. PMID:26595387

  15. Preparation of folic acid-conjugated, doxorubicin-loaded, magnetic bovine serum albumin nanospheres and their antitumor effects in vitro and in vivo

    Directory of Open Access Journals (Sweden)

    Yang R

    2014-09-01

    Full Text Available Rui Yang,1 YanLi An,2 FengQin Miao,1 MengFei Li,1 PeiDang Liu,1 QiuSha Tang1 1School of Medicine, Southeast University, 2Jiangsu Key Laboratory of Molecular and Functional Imaging, Department of Radiology, Zhongda Hospital, Nanjing, Jiangsu Province, People’s Republic of China Background: This study aimed to generate targeted folic acid-conjugated, doxorubicin-loaded, magnetic iron oxide bovine serum albumin nanospheres (FA-DOX-BSA MNPs that lower the side effects and improve the therapeutic effect of antitumor drugs when combined with hyperthermia and targeting therapy. A new nanodrug using magnetic nanospheres for heating and addition of the folate receptor with cancer cell specificity was prepared. The characteristics of these nanospheres and their antitumor effects in nasopharyngeal carcinoma were explored. Methods: FA-DOX-BSA MNPs comprising encapsulated magnetic iron oxide nanoparticles were prepared using a desolvation cross-linking method. Activated folic acid (N-hydroxysuccinimide ester of folic acid was conjugated to the surface of albumin nanospheres via amino groups.Results: Folic acid was successfully expressed on the surface of the nanospheres. Electron microscopy revealed that the FA-DOX-BSA MNPs were nearly spherical and uniform in size, with an average diameter of 180 nm. The nanomaterial could deliver doxorubicin at clinically relevant doses with an entrapment efficiency of 80%. An increasing temperature test revealed that incorporation of magnetic iron oxide into nanospheres could achieve a satisfactory heat treatment temperature at a significantly lower dose when placed in a high-frequency alternating magnetic field. FA-DOX-BSA MNPs showed greater inhibition of tumors than in the absence of folic acid in vitro and in vivo. Compared with chemotherapy alone, hyperthermia combined with chemotherapy was more effective against tumor cells.Conclusion: Folic acid-conjugated bovine serum albumin nanospheres composed of mixed

  16. BSA 500 UOP Course Tutorial/TutorialRank

    OpenAIRE

    apj

    2015-01-01

    For more course tutorials visit   www.tutorialrank.com   Tutorial Purchased: 4 Times, Rating: A+           BSA 500 Week 1 Learning Team Charter (UOP Course) BSA 500 Week 2 Individual Assignment Virtual Organizations Table Part I (UOP Course) BSA 500 Week 3 Individual Assignment Table 1 Part 2 Virtual Organization (UOP Course) BSA 500 Week 4 Individual Assingment Balance Sheet and Income Statement (UOP Cours...

  17. Interaction of coffee compounds with serum albumins. Part II: Diterpenes.

    Science.gov (United States)

    Guercia, Elena; Forzato, Cristina; Navarini, Luciano; Berti, Federico

    2016-05-15

    Cafestol and 16-O-methylcafestol are diterpenes present in coffee, but whilst cafestol is found in both Coffea canephora and Coffea arabica, 16-O-methylcafestol (16-OMC) was reported to be specific of only C. canephora. The interactions of such compounds, with serum albumins, have been studied. Three albumins have been considered, namely human serum albumin (HSA), fatty acid free HSA (ffHSA) and bovine serum albumin (BSA). The proteins interact with the diterpenes at the interface between Sudlow site I and the fatty acid binding site 6 in a very peculiar way, leading to a significant change in the secondary structure. The diterpenes do not displace reference binding drugs of site 2, but rather they enhance the affinity of the site for the drugs. They, therefore, may alter the pharmacokinetic profile of albumin - bound drugs. PMID:26776001

  18. Albumin extravasation rates in tissues of anesthetized and unanesthetized rats

    International Nuclear Information System (INIS)

    Bovine serum albumin (BSA) labeled with 131I was injected intravenously in chronically prepared, unanesthetized rats and into pentobarbital-anesthetized rats that had received 2 ml 5% BSA to help sustain plasma volume. Initial uptake rates (clearances) in skin, skeletal muscles, diaphragm, and heart (left ventricle) were measured over 1 h. BSA labeled with 125I was injected terminally to correct for intravascular 131I-BSA. Observed clearances were in the following order in both groups of animals: heart much greater than diaphragm approximately equal to skin greater than resting skeletal muscles. Differences between unanesthetized and anesthetized animals were small and inconsistently directed. Our results suggest that the lower albumin clearances reported in the literature for anesthetized rats are not the result of their immobility or any direct effect of anesthesia on albumin transport in these tissues. The lower transport rates appear to result indirectly from changes produced by anesthesia and/or surgery in controllable parameters such as plasma volume and intravascular protein mass

  19. Protein-directed in situ synthesis of platinum nanoparticles with superior peroxidase-like activity, and their use for photometric determination of hydrogen peroxide

    International Nuclear Information System (INIS)

    Platinum nanoparticles (Pt-NPs) with sizes in the range from 10 to 30 nm were synthesized using protein-directed one-pot reduction. The model globular protein bovine serum albumin (BSA) was exploited as the template, and the resulting BSA/Pt-NPs were studied by transmission electron microscopy, energy dispersive X-ray spectroscopy, and resonance Rayleigh scattering spectroscopy. The modified nanoparticles display a peroxidase-like activity that was exploited in a rapid method for the colorimetric determination of hydrogen peroxide which can be detected in the 50 μM to 3 mM concentration range. The limit of detection is 7.9 μM, and the lowest concentration that can be visually detected is 200 μM. (author)

  20. Self-assembled Biodegradable Nanoparticles and Polysaccharides as Biomimetic ECM Nanostructures for the Synergistic effect of RGD and BMP-2 on Bone Formation.

    Science.gov (United States)

    Wang, Zhenming; Dong, Li; Han, Lu; Wang, Kefeng; Lu, Xiong; Fang, Liming; Qu, Shuxin; Chan, Chun Wai

    2016-01-01

    Producing biomimetic extracellular matrix (ECM) is an effective approach to improve biocompatibility of medical devices. In this study, biomimetic ECM nanostructures are constructed through layer-by-layer self-assembling positively charged chitosan (Chi), negatively charged oxidized sodium alginate (OAlg), and positively charged bovine serum albumin (BSA)-based nanoparticles. The BSA-based nanoparticles in the self-assembled films not only result in porous nanostructures similar to natural ECM, but also preserve the activity and realize the sustained release of Bone morphogenetic protein-2 (BMP-2). The results of bone marrow stem cells (BMSCs) culture demonstrate that the penta-peptide glycine-arginine-glycine-aspartate-serine (GRGDS) grafted Chi/OAlg films favor cell adhesion and proliferation. GRGDS and BMP-2 in biomimetic ECM nanostructures synergistically promote BMSC functions and new bone formation. The RGD and BMP incorporated biomimetic ECM coatings could be applied on a variety of biomedical devices to improve the bioactivity and biocompatibility. PMID:27121121

  1. Self-assembled Biodegradable Nanoparticles and Polysaccharides as Biomimetic ECM Nanostructures for the Synergistic effect of RGD and BMP-2 on Bone Formation

    Science.gov (United States)

    Wang, Zhenming; Dong, Li; Han, Lu; Wang, Kefeng; Lu, Xiong; Fang, Liming; Qu, Shuxin; Chan, Chun Wai

    2016-01-01

    Producing biomimetic extracellular matrix (ECM) is an effective approach to improve biocompatibility of medical devices. In this study, biomimetic ECM nanostructures are constructed through layer-by-layer self-assembling positively charged chitosan (Chi), negatively charged oxidized sodium alginate (OAlg), and positively charged bovine serum albumin (BSA)-based nanoparticles. The BSA-based nanoparticles in the self-assembled films not only result in porous nanostructures similar to natural ECM, but also preserve the activity and realize the sustained release of Bone morphogenetic protein-2 (BMP-2). The results of bone marrow stem cells (BMSCs) culture demonstrate that the penta-peptide glycine-arginine-glycine-aspartate-serine (GRGDS) grafted Chi/OAlg films favor cell adhesion and proliferation. GRGDS and BMP-2 in biomimetic ECM nanostructures synergistically promote BMSC functions and new bone formation. The RGD and BMP incorporated biomimetic ECM coatings could be applied on a variety of biomedical devices to improve the bioactivity and biocompatibility. PMID:27121121

  2. Mesoporous silica nanoparticles with bilayer coating of poly(acrylic acid-co-itaconic acid) and human serum albumin (HSA): A pH-sensitive carrier for gemcitabine delivery.

    Science.gov (United States)

    Pourjavadi, Ali; Tehrani, Zahra Mazaheri

    2016-04-01

    Novel bilayer coated mesoporous silica nanoparticle (MCM-41) based on pH sensitive poly(acrylic acid-co-itaconic acid) and human serum albumin (HSA) was designed for controlled delivery of gemcitabine (anticancer drug) to cancer cells. The shell around the mesoporous silica has bilayer structure. Poly(acrylic acid-co-itaconic acid) was used as pH-sensitive inner shell and human serum albumin, HSA, was used as outer shell. The core-shell structure was formed due to electrostatic interaction between ammonium groups of modified MCM-41 and carboxylate groups of copolymer. Also, the albumin layer was wrapped around the copolymer coated nanoparticle by electrostatic interaction between ammonium groups from protein and carboxylate ions of copolymer shell. Moreover, the maximum release occurred at pH 5.5 (pH of endosomes) because the bilayer shell collapsed at this pH. The drug nanocarrier would be a good candidate for tumor therapy due to its biocompatibility, controlled release and pH responsive behavior. PMID:26838909

  3. Spectroscopic studies on the interaction of bovine serum albumin with Ginkgol C15:1 from Ginkgo biloba L

    Energy Technology Data Exchange (ETDEWEB)

    Fang, Yang-Yang [School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013 (China); School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang 212013 (China); Yang, Xiao-Ming, E-mail: XM_Yang1963@126.com [School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013 (China); Li, Yue-Ying [School of Medical Science and Laboratory Medicine, Jiangsu University, Zhenjiang 212013 (China); Feng, Chun-Lai [School of Pharmacy, Jiangsu University, Zhenjiang 212013 (China)

    2015-06-15

    The interaction between Ginkgol C15:1 (Ginkgol), a natural bioactive compound from Ginkgo biloba, and bovine serum albumin (BSA) was studied by fluorescence, UV–vis absorption, Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopy under simulative physiological conditions. The results showed that the fluorescence quenching of BSA by Ginkgol was a static quenching procedure through forming a 1:1 ground-state Ginkgol–BSA complex with a binding constant of about 2.6×10{sup 3} L mol{sup −1}. The values of the thermodynamic parameters indicated that electrostatic and hydrophobic forces played important roles in the interaction of BSA with Ginkgol. The binding distance between BSA and Ginkgol was 3.37 nm, based on Föster’s non-radiative energy transfer theory, and subdomain IIA (Sudlow site I) was the primary binding site which was consistent with that results of molecular docking modeling. The results of UV–vis, CD, three-dimensional fluorescence and FT-IR spectra indicated that binding of Ginkgol to BSA induced conformational changes of BSA. - Highlights: • This is the first time to report the interaction between Ginkgol C15:1 and BSA. • Researching the binding properties of Ginkgol C15:1 and BSA in-depth. • From the aspect of BSA structure change, verified the anticancer activity of Ginkgol. • Molecular docking study explored the interaction of Ginkgol on BSA.

  4. Spectroscopic studies on the interaction of bovine serum albumin with Ginkgol C15:1 from Ginkgo biloba L

    International Nuclear Information System (INIS)

    The interaction between Ginkgol C15:1 (Ginkgol), a natural bioactive compound from Ginkgo biloba, and bovine serum albumin (BSA) was studied by fluorescence, UV–vis absorption, Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopy under simulative physiological conditions. The results showed that the fluorescence quenching of BSA by Ginkgol was a static quenching procedure through forming a 1:1 ground-state Ginkgol–BSA complex with a binding constant of about 2.6×103 L mol−1. The values of the thermodynamic parameters indicated that electrostatic and hydrophobic forces played important roles in the interaction of BSA with Ginkgol. The binding distance between BSA and Ginkgol was 3.37 nm, based on Föster’s non-radiative energy transfer theory, and subdomain IIA (Sudlow site I) was the primary binding site which was consistent with that results of molecular docking modeling. The results of UV–vis, CD, three-dimensional fluorescence and FT-IR spectra indicated that binding of Ginkgol to BSA induced conformational changes of BSA. - Highlights: • This is the first time to report the interaction between Ginkgol C15:1 and BSA. • Researching the binding properties of Ginkgol C15:1 and BSA in-depth. • From the aspect of BSA structure change, verified the anticancer activity of Ginkgol. • Molecular docking study explored the interaction of Ginkgol on BSA

  5. Spectroscopy and Fluorescence Lifetime Imaging Microscopy To Probe the Interaction of Bovine Serum Albumin with Graphene Oxide.

    Science.gov (United States)

    Kuchlyan, Jagannath; Kundu, Niloy; Banik, Debasis; Roy, Arpita; Sarkar, Nilmoni

    2015-12-29

    The interaction of graphene oxide (GO) with bovine serum albumin (BSA) in aqueous buffer solution has been investigated with various spectroscopic and imaging techniques. At single molecular resolution this interaction has been performed using fluorescence correlation spectroscopy (FCS) and fluorescence lifetime imaging microscopy (FLIM) techniques. The conformational dynamics of BSA on GO's influence have been explored by FCS and circular dichroism (CD) spectroscopy. For the FCS studies BSA was labeled covalently by a fluorophore, Alexa Fluor 488. On the addition of GO in phosphate buffer of 10 mM at pH 7.4 the diffusion time (τD) and the hydrodynamic radius (Rh) of BSA increase due to adsorption of BSA. Conformational relaxation time components of native BSA drastically vary with the addition of GO, signifying the change of conformational dynamics of BSA after addition of GO. The adsorption isotherm also indicates significant adsorption of BSA on the GO surface. Adsorption of BSA on the GO surface has shown in direct images of atomic force microscopy (AFM) and FLIM. Fluorescence quenching study of BSA with addition of GO also indicates that there is strong interaction between BSA and GO. PMID:26646418

  6. Characterization of 6-mercaptopurine binding to bovine serum albumin and its displacement from the binding sites by quercetin and rutin

    Energy Technology Data Exchange (ETDEWEB)

    Ehteshami, Mehdi [Nutrition Research Center, School of Health and Nutrition, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of); Rasoulzadeh, Farzaneh [Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of); Mahboob, Soltanali [Nutrition Research Center, School of Health and Nutrition, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of); Rashidi, Mohammad-Reza, E-mail: rashidi@tbzmed.ac.ir [Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of)

    2013-03-15

    Binding of a drug to the serum albumins as major serum transport proteins can be influenced by other ligands leading to alteration of its pharmacological properties. In the present study, binding characteristics of 6-mercaptopurine (6-MP) with bovine serum albumin (BSA) together with its displacement from its binding site by quercetin and rutin have been investigated by the spectroscopic method. According to the binding parameters, a static quenching component in overall dynamic quenching process is operative in the interaction between 6-MP and BSA. The binding of 6-MP to BSA occurred spontaneously due to entropy-driven hydrophobic interactions. The synchronous fluorescence spectroscopy study revealed that the secondary structure of BSA is changed in the presence of 6-MP and both Tyr and Trp residues participate in the interaction between 6-MP and BSA with the later one being more dominant. The binding constant value of 6-MP-BSA in the presence of quercetin and rutin increased. 6-MP was displaced by ibuprofen indicating that the binding site of 6-MP on albumin is site II. Therefore, the change of the pharmacokinetic and pharmacodynamic properties of 6-MP by quercetin and rutin through alteration of binding capacity of 6-MP to the serum albumin cannot be ruled out. In addition, the displacement study showed that 6-MP is located in site II of BSA. - Highlights: Black-Right-Pointing-Pointer Participation of both Tyr and particularly Trp residues in the interaction between 6-MP and BSA. Black-Right-Pointing-Pointer Involvement of a static quenching component in an overall dynamic quenching process. Black-Right-Pointing-Pointer Ability of quercetin and rutin to change the binding constants of 6-MP-BSA complex. Black-Right-Pointing-Pointer Binding of 6-MP to BSA through entropy-driven hydrophobic interactions.

  7. Characterization of 6-mercaptopurine binding to bovine serum albumin and its displacement from the binding sites by quercetin and rutin

    International Nuclear Information System (INIS)

    Binding of a drug to the serum albumins as major serum transport proteins can be influenced by other ligands leading to alteration of its pharmacological properties. In the present study, binding characteristics of 6-mercaptopurine (6-MP) with bovine serum albumin (BSA) together with its displacement from its binding site by quercetin and rutin have been investigated by the spectroscopic method. According to the binding parameters, a static quenching component in overall dynamic quenching process is operative in the interaction between 6-MP and BSA. The binding of 6-MP to BSA occurred spontaneously due to entropy-driven hydrophobic interactions. The synchronous fluorescence spectroscopy study revealed that the secondary structure of BSA is changed in the presence of 6-MP and both Tyr and Trp residues participate in the interaction between 6-MP and BSA with the later one being more dominant. The binding constant value of 6-MP–BSA in the presence of quercetin and rutin increased. 6-MP was displaced by ibuprofen indicating that the binding site of 6-MP on albumin is site II. Therefore, the change of the pharmacokinetic and pharmacodynamic properties of 6-MP by quercetin and rutin through alteration of binding capacity of 6-MP to the serum albumin cannot be ruled out. In addition, the displacement study showed that 6-MP is located in site II of BSA. - Highlights: ► Participation of both Tyr and particularly Trp residues in the interaction between 6-MP and BSA. ► Involvement of a static quenching component in an overall dynamic quenching process. ► Ability of quercetin and rutin to change the binding constants of 6-MP–BSA complex. ► Binding of 6-MP to BSA through entropy-driven hydrophobic interactions

  8. Long-Term Toxicity of 213Bi-Labelled BSA in Mice.

    Directory of Open Access Journals (Sweden)

    Laëtitia Dorso

    Full Text Available Short-term toxicological evaluations of alpha-radioimmunotherapy have been reported in preclinical assays, particularly using bismuth-213 (213Bi. Toxicity is greatly influenced not only by the pharmacokinetics and binding specificity of the vector but also by non-specific irradiation due to the circulating radiopharmaceutical in the blood. To assess this, an acute and chronic toxicity study was carried out in mice injected with 213Bi-labelled Bovine Serum Albumin (213Bi-BSA as an example of a long-term circulating vector.Biodistribution of 213Bi-BSA and 125I-BSA were compared in order to evaluate 213Bi uptake by healthy organs. The doses to organs for injected 213Bi-BSA were calculated. Groups of nude mice were injected with 3.7, 7.4 and 11.1 MBq of 213Bi-BSA and monitored for 385 days. Plasma parameters, including alanine aminotransferase (ALT, aspartate aminotransferase (AST, blood urea nitrogen (BUN and creatinine, were measured and blood cell counts (white blood cells, platelets and red blood cells were performed. Mouse organs were examined histologically at different time points.Haematological toxicity was transient and non-limiting for all evaluated injected activities. At the highest injected activity (11.1 MBq, mice died from liver and kidney failure (median survival of 189 days. This liver toxicity was identified by an increase in both ALT and AST and by histological examination. Mice injected with 7.4 MBq of 213Bi-BSA (median survival of 324 days had an increase in plasma BUN and creatinine due to impaired kidney function, confirmed by histological examination. Injection of 3.7 MBq of 213Bi-BSA was safe, with no plasma enzyme modifications or histological abnormalities.Haematological toxicity was not limiting in this study. Liver failure was observed at the highest injected activity (11.1 MBq, consistent with liver damage observed in human clinical trials. Intermediate injected activity (7.4 MBq should be used with caution because of

  9. Preparation and properties of BSA-loaded microspheres based on multi-(amino acid copolymer for protein delivery

    Directory of Open Access Journals (Sweden)

    Chen X

    2014-05-01

    Full Text Available Xingtao Chen,1 Guoyue Lv,1 Jue Zhang,2 Songchao Tang,2 Yonggang Yan,1 Zhaoying Wu,2 Jiacan Su,2 Jie Wei2 1College of Physical Science and Technology, Sichuan University, Chengdu, 2Key Laboratory for Ultrafine Materials of Ministry of Education, East China University of Science and Technology, Shanghai, People’s Republic of China Abstract: A multi-(amino acid copolymer (MAC based on ω-aminocaproic acid, γ-aminobutyric acid, L-alanine, L-lysine, L-glutamate, and hydroxyproline was synthetized, and MAC microspheres encapsulating bovine serum albumin (BSA were prepared by a double-emulsion solvent extraction method. The experimental results show that various preparation parameters including surfactant ratio of Tween 80 to Span 80, surfactant concentration, benzyl alcohol in the external water phase, and polymer concentration had obvious effects on the particle size, morphology, and encapsulation efficiency of the BSA-loaded microspheres. The sizes of BSA-loaded microspheres ranged from 60.2 µm to 79.7 µm, showing different degrees of porous structure. The encapsulation efficiency of BSA-loaded microspheres also ranged from 38.8% to 50.8%. BSA release from microspheres showed the classic biphasic profile, which was governed by diffusion and polymer erosion. The initial burst release of BSA from microspheres at the first week followed by constant slow release for the next 7 weeks were observed. BSA-loaded microspheres could degrade gradually in phosphate buffered saline buffer with pH value maintained at around 7.1 during 8 weeks incubation, suggesting that microsphere degradation did not cause a dramatic pH drop in phosphate buffered saline buffer because no acidic degradation products were released from the microspheres. Therefore, the MAC microspheres might have great potential as carriers for protein delivery. Keywords: poly (amino acid copolymer, release, degradation

  10. Quantitative study of molecular transport due to electroporation: uptake of bovine serum albumin by erythrocyte ghosts.

    OpenAIRE

    Prausnitz, M.R.; Milano, C D; Gimm, J A; Langer, R; Weaver, J C

    1994-01-01

    Electroporation is believed to involve the creation of aqueous pathways in lipid bilayer membranes by transient elevation of the transmembrane voltage to approximately 1 V. Here, results are presented for a quantitative study of the number of bovine serum albumin (BSA) molecules transported into erythrocyte ghosts caused by electroportion. 1) Uptake of BSA was found to plateau at high field strength. However, this was not necessarily an absolute maximum in transport. Instead, it represented t...

  11. Study on the interaction between ketoprofen and bovine serum albumin by molecular simulation and spectroscopic methods

    OpenAIRE

    Zhu, Jin Lian; He, Jia; He, Hua; Tan, Shu Hua; He, Xiao Mei; Pham-Huy, Chuong; Li, Lun

    2011-01-01

    The interaction between ketoprofen and bovine serum albumin (BSA) was investigated by molecular simulation, fluorescence and UV-vis spectroscopy methods under the simulated physiological conditions. Molecular simulation method performed to reveal the possible binding mode or mechanism suggested the binding forces between ketoprofen and BSA were mainly hydrophobic interaction and hydrogen bond, which was in agreement with the thermodynamic study (ΔHΦ and ΔSΦ were calculated to be 74.514 kJ/mol...

  12. Characterization of the Interaction between Eupatorin and Bovine Serum Albumin by Spectroscopic and Molecular Modeling Methods

    OpenAIRE

    Guiying Li; Zhengqiang Li; Tianshi Wang; Haoran Xu; Nannan Yao; Hongliang Xu

    2013-01-01

    This study investigated the interaction between eupatorin and bovine serum albumin (BSA) using ultraviolet-visible (UV-vis) absorption, fluorescence, synchronous fluorescence, circular dichroism (CD) spectroscopies, and molecular modeling at pH 7.4. Results of UV-vis and fluorescence spectroscopies illustrated that BSA fluorescence was quenched by eupatorin via a static quenching mechanism. Thermodynamic parameters revealed that hydrophobic and electrostatic interactions played major roles in...

  13. Glycation of bovine serum albumin by ascorbate in vitro: Possible contribution of the ascorbyl radical?

    OpenAIRE

    Sadowska-Bartosz, Izabela; Stefaniuk, Ireneusz; Galiniak, Sabina; Bartosz, Grzegorz

    2015-01-01

    Ascorbic acid (AA) has been reported to be both pro-and antiglycating agent. In vitro, mainly proglycating effects of AA have been observed. We studied the glycation of bovine serum albumin (BSA) induced by AA in vitro. BSA glycation was accompanied by oxidative modifications, in agreement with the idea of glycoxidation. Glycation was inhibited by antioxidants including polyphenols and accelerated by 2,​2′-​azobis-​2-​methyl-​propanimidamide and superoxide dismutase. Nitroxides, known to oxid...

  14. Structural Relationship and Binding Mechanisms of Five Flavonoids with Bovine Serum Albumin

    OpenAIRE

    Ping Li; E-Hu Liu; Lian-Wen Qi

    2010-01-01

    Flavonoids are structurally diverse and the most ubiquitous groups of dietary polyphenols distributed in various fruits and vegetables. In this study, the interaction between five flavonoids, namely formononetin-7-O-β-D-glucoside, calycosin- 7-O-β-D-glucoside, calycosin, rutin, and quercetin, and bovine serum albumin (BSA) was investigated by fluorescence and UV-vis absorbance spectroscopy. In the discussion, it was proved that the fluorescence quenching of BSA by flavonoids was a result of t...

  15. Detection and analysis of human serum albumin nanoparticles within phagocytic cells at the resolution of individual live cell or single 3D multicellular spheroid

    International Nuclear Information System (INIS)

    Since nanoparticles (NPs) have shown great potential in various biomedical applications, live cell response to NPs should be thoroughly explored prior to their in vivo use. In the current study, live cell array (LCA) methodology and unique cell-based assays were used to study the interaction of magnetite (HSA-Mag NP) loaded human serum albumin NPs with phagocytic cells. The LCA enabled cell culturing during HSA-Mag NP accumulation and monolayer or spheroid formation, concomitantly with on-line monitoring of NP internalization. These platforms were also utilized for imaging intercellular links between living cells preloaded with HSA-Mag NP in 2D and 3D resolution. HSA-Mag NP uptake by cells was quantified by imaging, and analyzed using time-resolved measurements. Image analysis of the individual cells in cell populations showed accumulation of HSA-Mag NP by promonocytes and glial cells in a dose- and time-dependent manner. High variability of NP accumulation in individual cells within cell populations, as well as cell subgroups, was evident in both cell types. Following 24 h interaction, uptake of HSA-Mag NP was about 10 times more efficient in glial cells than in activated promonocytes. The presented assays may facilitate detection and analysis of the amount of NPs within individual cells, as well as the rate of NP accumulation and processing in different subsets of living cells. Such data are crucial for estimating predicted drug dosage delivered by NPs, as well as to study possible mechanisms for NP interference with live cells

  16. Detection and analysis of human serum albumin nanoparticles within phagocytic cells at the resolution of individual live cell or single 3D multicellular spheroid

    Energy Technology Data Exchange (ETDEWEB)

    Afrimzon, Elena; Zurgil, Naomi; Sobolev, Maria; Shafran, Yana [Bar-Ilan University, The Biophysical Interdisciplinary Schottenstein Center for the Research and Technology of the Cellome (Israel); Langer, Klaus; Zlatev, Iavor [Westfälischen Wilhelms-Universität Münster, Institut für Pharmazeutische Technologie und Biopharmazie (Germany); Wronski, Robert; Windisch, Manfred [QPS Austria GmbH (Austria); Briesen, Hagen von [Fraunhofer Institute for Biomedical Engineering IBMT, Department of Cell Biology & Applied Virology (Germany); Schmidt, Reinhold [Medical University of Graz, Department of Neurology (Austria); Pietrzik, Claus [University Medical Center of the Johannes Gutenberg University of Mainz, Institute of Pathobiochemistry (Germany); Deutsch, Mordechai, E-mail: motti.jsc@gmail.com [Bar-Ilan University, The Biophysical Interdisciplinary Schottenstein Center for the Research and Technology of the Cellome (Israel)

    2015-12-15

    Since nanoparticles (NPs) have shown great potential in various biomedical applications, live cell response to NPs should be thoroughly explored prior to their in vivo use. In the current study, live cell array (LCA) methodology and unique cell-based assays were used to study the interaction of magnetite (HSA-Mag NP) loaded human serum albumin NPs with phagocytic cells. The LCA enabled cell culturing during HSA-Mag NP accumulation and monolayer or spheroid formation, concomitantly with on-line monitoring of NP internalization. These platforms were also utilized for imaging intercellular links between living cells preloaded with HSA-Mag NP in 2D and 3D resolution. HSA-Mag NP uptake by cells was quantified by imaging, and analyzed using time-resolved measurements. Image analysis of the individual cells in cell populations showed accumulation of HSA-Mag NP by promonocytes and glial cells in a dose- and time-dependent manner. High variability of NP accumulation in individual cells within cell populations, as well as cell subgroups, was evident in both cell types. Following 24 h interaction, uptake of HSA-Mag NP was about 10 times more efficient in glial cells than in activated promonocytes. The presented assays may facilitate detection and analysis of the amount of NPs within individual cells, as well as the rate of NP accumulation and processing in different subsets of living cells. Such data are crucial for estimating predicted drug dosage delivered by NPs, as well as to study possible mechanisms for NP interference with live cells.

  17. Interaction of glutathione with bovine serum albumin: Spectroscopy and molecular docking.

    Science.gov (United States)

    Jahanban-Esfahlan, Ali; Panahi-Azar, Vahid

    2016-07-01

    This study aims to investigate the interaction between glutathione and bovine serum albumin (BSA) using ultraviolet-visible (UV-vis) absorption, fluorescence spectroscopies under simulated physiological conditions (pH 7.4) and molecular docking methods. The results of fluorescence spectroscopy indicated that the fluorescence intensity of BSA was decreased considerably upon the addition of glutathione through a static quenching mechanism. The fluorescence quenching obtained was related to the formation of BSA-glutathione complex. The values of KSV, Ka and Kb for the glutathione and BSA interaction were in the order of 10(5). The thermodynamic parameters including enthalpy change (ΔH), entropy change (ΔS) and also Gibb's free energy (ΔG) were determined using Van't Hoff equation. These values showed that hydrogen bonding and van der Waals forces were the main interactions in the binding of glutathione to BSA and the stabilization of the complex. Also, the interaction of glutathione and BSA was spontaneous. The effects of glutathione on the BSA conformation were determined using UV-vis spectroscopy. Moreover, glutathione was docked in BSA using ArgusLab as a molecular docking program. It was recognized that glutathione binds within the sub-domain IIA pocket in domain II of BSA. PMID:26920314

  18. Spectroscopic studies on the interaction between chalcone and bovine serum albumin

    International Nuclear Information System (INIS)

    The interaction between chalcone and bovine serum albumin (BSA) has been studied by spectroscopic techniques under physiological condition. By the analysis of fluorescence spectrum and fluorescence intensity, it was observed that the chalcone has a strong ability to quench the intrinsic fluorescence with BSA through a static quenching procedure and non-radiation energy transfer were the main reasons for the fluorescence quenching. The association constants of chalcone with BSA were determined at different temperatures based on fluorescence quenching results. The positive entropy change and enthalpy change indicated that the interaction of chalcone and BSA was driven mainly by hydrophobic forces. The process of binding was a spontaneous process in which Gibbs free energy change was negative. The distance, r, between donor (BSA) and acceptor (chalcone) was obtained according to the Forster's theory of non-radiation energy transfer. The UV–vis, CD, FT-IR, synchronous and 3-D spectral results revealed the changes in the secondary structure of BSA upon interaction with chalcone. The effects of some common metal ions on binding of BSA–chalcone complex were also investigated. -- Highlights: • We explored the interaction between chalcone and BSA by fluorescence spectroscopy. • The fluorescence quenching mechanism was static quenching. • The binding constants and thermodynamic parameters were calculated. • The interaction is driven mainly by hydrophobic force. • The binding of chalcone to BSA induced changes in the secondary structure of BSA

  19. A spectroscopic study on the interaction between p-nitrophenol and bovine serum albumin

    International Nuclear Information System (INIS)

    The interaction between p-nitrophenol (PNP) with bovine serum albumin (BSA) was investigated by fluorescence quenching, UV–visible absorption, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy under the simulative physiological conditions. It is found that PNP has a strong ability to quench the intrinsic fluorescence of BSA by forming a 1:1 ground-state complex with a binding constant of about 104 L mol−1. The values of the calculated thermodynamic parameters suggest that hydrogen bonds and hydrophobic forces played major roles in stabilizing the complex. The displacement experiments indicate that the binding of PNP to BSA primarily occurred in the sub-domain IIA (site I) of BSA. The binding distance r was calculated to be 1.58 nm based on the theory of Förster's non-radiation energy transfer. The analysis of synchronous fluorescence, FT-IR, CD, and three-dimensional fluorescence spectra reveals that the microenvironment of amino acid residues and the conformation of BSA were changed after addition of PNP. - Highlights: • Multi-spectroscopy techniques were used to study the interactions between PNP and BSA. • PNP has a strong ability to quench the intrinsic fluorescence of BSA by forming a 1:1 ground state complex. • Hydrogen bond and hydrophobic forces played major roles in the binding of PNP with BSA. • The microenvironment of amino acid residues and the conformation of BSA were changed upon addition of PNP

  20. A feasible synthesis of Mn3(PO4)2@BSA nanoflowers and its application as the support nanomaterial for Pt catalyst

    Science.gov (United States)

    Zhang, Zhihong; Zhang, Yuanchang; He, Linghao; Yang, Yanqin; Liu, Shunli; Wang, Minghua; Fang, Shaoming; Fu, Guodong

    2015-06-01

    We report the production of a novel nanoflower material of Mn3(PO4)2@BSA hybrid which is made of both protein and manganese (II) phosphate, and its application as a new support material for platinum nanoparticles (PtNPs). The Mn3(PO4)2@BSA@PtNPs catalyst is synthesized using this new material. The average size of PtNPs on the Mn3(PO4)2@BSA nanoflower is approximately 2 nm. The obtained Mn3(PO4)2@BSA@PtNPs nanocomposites are characterized by X-ray diffraction, high resolution transmission electron microscopy, and scanning electron microscopy. Electrochemical results show that the Mn3(PO4)2@BSA@PtNPs catalyst also shows excellent electrocatalytic activity toward methanol oxidation with higher electrochemically active surface area. The microstructure of the supporting material serves a crucial function in the electrochemical performance of the Pt-based catalyst.

  1. Interaction of some cardiovascular drugs with bovine serum albumin at physiological conditions using glassy carbon electrode: A new approach.

    Science.gov (United States)

    Afsharan, Hadi; Hasanzadeh, Mohammad; Shadjou, Nasrin; Jouyban, Abolghasem

    2016-08-01

    In this report, for the first time, the non-modified glassy carbon electrode was used for detection of cardiovascular drug interaction with bovine serum albumin (BSA). These interactions were tested at physiological conditions (T=37°C and pH=7.4 phosphate buffer solution) in different incubation times (0-4h) by cyclic voltammetry (CV), differential pulse voltammetry (DPV) and square wave voltammetry (SWV). The applications of DPV for quantitative investigation of some cardiovascular drug interaction with BSA (as a model of serum albumin proteins) were discussed. The herein described approach is expected to promote the exploitation of electrochemically-based methods for the study of drug-serum albumin protein interaction which is necessary in biochemical and biosensing studies. This report may open a new window to application of electrochemical sensors towards interactions of cardiovascular drugs with BSA and human serum albumin (HAS) in the near future. PMID:27157732

  2. Interaction of the flavonoid hesperidin with bovine serum albumin: A fluorescence quenching study

    International Nuclear Information System (INIS)

    The interaction between the flavonoid hesperidin and bovine serum albumin (BSA) was investigated by fluorescence and UV/Vis absorption spectroscopy. The results revealed that hesperidin caused the fluorescence quenching of BSA through a static quenching procedure. The hydrophobic and electrostatic interactions play a major role in stabilizing the complex. The binding site number n, and apparent binding constant K A, corresponding thermodynamic parameters ΔG o, ΔH o, ΔS o at different temperatures were calculated. The distance r between donor (BSA) and acceptor (hesperidin) was obtained according to fluorescence resonance energy transfer. The effect of Cu2+, Zn2+, Ni2+, Co2+, and Mn2+ on the binding constants between hesperidin and BSA were studied. The effect of hesperidin on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy and UV/Vis absorption spectroscopy

  3. Fluorescence study on the interactions of PAMAM dendrimers and their derivatives with bovine serum albumin

    Institute of Scientific and Technical Information of China (English)

    WANG Yanming; SONG Yu; KONG Deling; YU Yaoting

    2005-01-01

    The interactions of amino-terminated, and ethylenediamine core poly(amidoamine) (PAMAM) dendrimers and their derivatives with bovine serum albumin (BSA) were investigated by fluorescence spectroscopy. Experimental results showed that the fluorescence intensity of BSA decreased after the addition of different modified dendrimers, and the extent of the fluorescence quenching caused by various modified dendrimers strongly depends upon the different functional groups on their surfaces. We also investigated the influence of pH and ionic strength on the interaction between various modified dendrimers and BSA. Circular dichroism (CD) spectroscopic measurements showed that the content of α-helix structure of BSA decreased after the addition of different modified dendrimers, which indicated that dendrimers induced changes in the secondary structure of BSA.

  4. Interaction of bovine serum albumin protein with self assembled monolayer of mercaptoundecanoic acid

    Science.gov (United States)

    Poonia, Monika; Agarwal, Hitesh; Manjuladevi, V.; Gupta, R. K.

    2016-05-01

    Detection of proteins and other biomolecules in liquid phase is the essence for the design of a biosensor. The sensitivity of a sensor can be enhanced by the appropriate functionalization of the sensing area so as to establish the molecular specific interaction. In the present work, we have studied the interaction of bovine serum albumin (BSA) protein with a chemically functionalized surface using a quartz crystal microbalance (QCM). The gold-coated quartz crystals (AT-cut/5 MHz) were functionalized by forming self-assembled monolayer (SAM) of 11-Mercaptoundecanoic acid (MUA). The adsorption characteristics of BSA onto SAM of MUA on quartz crystal are reported. BSA showed the highest affinity for SAM of MUA as compared to pure gold surface. The SAM of MUA provides carboxylated surface which enhances not only the adsorption of the BSA protein but also a very stable BSA-MUA complex in the liquid phase.

  5. An Efficient Cryptographic Hash Algorithm (BSA)

    CERN Document Server

    Mukherjee, Subhabrata; Laha, Anirban

    2012-01-01

    Recent cryptanalytic attacks have exposed the vulnerabilities of some widely used cryptographic hash functions like MD5 and SHA-1. Attacks in the line of differential attacks have been used to expose the weaknesses of several other hash functions like RIPEMD, HAVAL. In this paper we propose a new efficient hash algorithm that provides a near random hash output and overcomes some of the earlier weaknesses. Extensive simulations and comparisons with some existing hash functions have been done to prove the effectiveness of the BSA, which is an acronym for the name of the 3 authors.

  6. Interaction of Surface-active Fluorescence Probes with Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    Tong Kuan XU; Xing Hai SHEN; Na LI; Hong Cheng GAO

    2005-01-01

    The binding between three surface-active substituted 3H-indole fluorescence probes and bovine serum albumin (BSA) in aqueous solution was studied using fluorescence quenching. The binding constants of 3H-indole molecules with BSA were obtained. According to the Forster resonance energy transfer theory, the distances between 3H-indole molecules and tryptophan of BSA were calculated. The results show that the oligoethyloxyethylene chain of 3H-indole molecules is longer, the binding between them is stronger, the energy transfer efficiency is higher,and the distance between tryptophan and 3H-indole is nearer.

  7. Determination of protein-ligand binding affinity by NMR: observations from serum albumin model systems.

    Science.gov (United States)

    Fielding, Lee; Rutherford, Samantha; Fletcher, Dan

    2005-06-01

    The usefulness of bovine serum albumin (BSA) as a model protein for testing NMR methods for the study of protein-ligand interactions is discussed. Isothermal titration calorimetry established the binding affinity and stoichiometry of the specific binding site for L-tryptophan, D-tryptophan, naproxen, ibuprofen, salicylic acid and warfarin. The binding affinities of the same ligands determined by NMR methods are universally weaker (larger KD). This is because the NMR methods are susceptible to interference from additional non-specific binding. The L-tryptophan-BSA and naproxen-BSA systems were the best behaved model systems. PMID:15816062

  8. Relief of amplification inhibition in PCR with bovine serum albumin or T4 gene 32 protein.

    OpenAIRE

    Kreader, C A

    1996-01-01

    The benefits of adding bovine serum albumin (BSA) or T4 gene 32 protein (gp32) to PCR were evaluated with reaction mixtures containing substances that inhibit amplification. Whereas 10- to 1,000-fold more FeCl3, hemin, fulvic acids, humic acids, tannic acids, or extracts from feces, freshwater, or marine water were accommodated in PCR when either 400 ng of BSA per microl or 150 ng of gp32 per microl was included in the reactions, neither BSA nor gp32 relieved interference significantly when m...

  9. Drug release mechanisms of chemically cross-linked albumin microparticles: effect of the matrix erosion

    OpenAIRE

    Sitta, Danielly L. A.; Guilherme, Marcos R.; Silva, Elisangela P. da; Valente, Artur J. M.; Edvani C. Muniz; Adley F. Rubira

    2014-01-01

    Albumin (BSA) microparticles were developed as a biotechnological alternative for drug delivery. Vitamin B12 (Vit-B12) was used as a model drug. The microparticles were obtained from maleic anhydride-functionalized BSA and N′,N′-dimethylacrylamide (DMAAm) in a W/O emulsion without and with PVA. The microparticles produced at 15 min of stirring without PVA showed the best results in terms of size, homogeneity, and sphericity. In such a case, BSA played a role as a surface active agent, replaci...

  10. Study on the interaction between clarithromycin and bovine serum albumin in the imitated physiology solution

    Institute of Scientific and Technical Information of China (English)

    She Ying Dong; Chun Xia Xue; Ting Lin Huang

    2007-01-01

    The interaction between clarithromycin (CAM) and bovine serum albumin (BSA) was investigated using linear-sweep voltammetry in pH 7.4 phosphate buffer solution where CAM caused two irreversible reduction waves P2 and P3 on mercury electrode.The study showed that the formation constant and formation ratio for the interaction between CAM and BSA were 1.51 x 1012 and 3:1 for P2,4.53 x 105 and 1:1 for P3, respectively.The ion strength enhanced the hydrophobic interaction between CAM and BSA.

  11. Aggregation and fibrillation of bovine serum albumin

    DEFF Research Database (Denmark)

    Holm, NK; Jespersen, SK; Thomassen, LV;

    2007-01-01

    The all-alpha helix multi-domain protein bovine serum albumin (BSA) aggregates at elevated temperatures. Here we show that these thermal aggregates have amyloid properties. They bind the fibril-specific dyes Thioflavin T and Congo Red, show elongated although somewhat worm-like morphology and...... characteristic amyloid X-ray fiber diffraction peaks. Fibrillation occurs over minutes to hours without a lag phase, is independent of seeding and shows only moderate concentration dependence, suggesting intramolecular aggregation nuclei. Nevertheless, multi-exponential increases in dye-binding signal and...

  12. Effects of perfluorooctane sulfonate on the conformation and activity of bovine serum albumin.

    Science.gov (United States)

    Wang, Yanqing; Zhang, Hongmei; Kang, Yijun; Cao, Jian

    2016-06-01

    Perfluorooctane sulfonate (PFOS) is among the most prominent contaminates in human serum and has been reported to possess potential toxicity to the human body. In this study, the effects of PFOS on the conformation and activity of bovine serum albumin (BSA) were investigated in vitro. The results indicated that the binding interaction of PFOS with BSA destroyed the tertiary and secondary structures of protein with the loss of α-helix structure and the increasing of hydrophobic microenvironment of the Trp or Tyr residues. During the thermal denaturation protein, PFOS increases the protein stability of BSA. The proportion of α-helix decreased on increasing the PFOS concentration and the microenvironment of the Trp or Tyr residues becomes more hydrophobic. The results from molecular modeling indicated that BSA had not only one possible binding site to bind with PFOS by the polar interaction, hydrogen bonds and hydrophobic forces. In addition, the BSA relative activities were decreased with the increase of PFOS concentration. Such loss of BSA activity in the presence of PFOS indicated that one of the binding sites in BSA is located in subdomain IIIA, which is in good agreement with the fluorescence spectroscopic experiments and molecular modeling results. This study offers a comprehensive picture of the interactions of PFOS with serum albumin and provides insights into the toxicological effect of perfluoroalkylated substances. PMID:27031195

  13. Interaction of Palmitic Acid with Metoprolol Succinate at the Binding Sites of Bovine Serum Albumin

    OpenAIRE

    Mashiur Rahman; Farzana Prianka; Mohammad Shohel; Md. Abdul Mazid

    2014-01-01

    Purpose: The aim of this study was to characterize the binding profile as well as to notify the interaction of palmitic acid with metoprolol succinate at its binding site on albumin. Methods: The binding of metoprolol succinate to bovine serum albumin (BSA) was studied by equilibrium dialysis method (ED) at 27°C and pH 7.4, in order to have an insight in the binding chemistry of the drug to BSA in presence and absence of palmitic acid. The study was carried out using ranitidine as site-1 a...

  14. Studies on the interaction between scopoletin and two serum albumins by spectroscopic methods

    Energy Technology Data Exchange (ETDEWEB)

    Cheng Zhengjun, E-mail: ncczj1112@126.com [Chemical Synthesis and Pollution Control Key Laboratory of Sichuan Province, China West Normal University, Nanchong 637002 (China)

    2012-10-15

    The interactions of scopoletin to bovine serum albumin (BSA) and human serum albumin (HSA) have been investigated by spectroscopic methods. The fluorescence tests indicated that the formation mechanism of scopoletin-BSA/HSA complexes belonged to the static quenching. The displacement experiments suggested that scopoletin primarily bound to tryptophan residues of BSA/HSA within site I (subdomain IIA). The binding distance of scopoletin to BSA/HSA was 2.38/2.34 nm. The thermodynamic parameters ({Delta}G, {Delta}H and {Delta}S) calculated on the basis of different temperatures revealed that the binding of BSA-scopoletin was mainly depended on van der Waals interaction and hydrogen bond, and yet the binding of HSA-scopoletin was strongly relied on the hydrophobic interaction and electrostatic interaction. The results of synchronous fluorescence, 3D fluorescence, UV-vis absorption, and FT-IR spectra showed that the conformations of BSA and HSA altered with the addition of scopoletin. In addition, the effects of some common ions on the binding constants of scopoletin to proteins were also investigated. - Highlights: Black-Right-Pointing-Pointer Binding modes of scopoletin to HSA/BSA have been established. Black-Right-Pointing-Pointer The binding sites on BSA/HSA by scopoletin were discussed. Black-Right-Pointing-Pointer Investigating the structural changes of HSA and BSA in the presence of scopoletin. Black-Right-Pointing-Pointer Energy transfer and the type of the binding forces were investigated for two systems. Black-Right-Pointing-Pointer Influences of common ions on the binding constants of BSA/HSA with scopoletin were investigated.

  15. Ilaprazole metabolites, ilaprazole sulfone and ilaprazole sulfide decreased the affinity of ilaprazole to bovine serum albumin

    International Nuclear Information System (INIS)

    The interaction of ilaprazole (IPZ), ilaprazole sulfone (IPZO) and ilaprazole sulfide (IPZI) with bovine serum albumin (BSA), and the effect of IPZO and IPZI on the interaction of IPZ with BSA have been investigated by fluorescence, synchronous fluorescence, ultraviolet–visible (UV–vis), Fourier transform infrared spectroscopy (FT-IR) and circular dichroism (CD). The results indicated that IPZ, IPZO and IPZI had a strong ability to quench the intrinsic fluorescence of BSA, and the binding affinities were significantly affected by structures in the order IPZ>IPZO>IPZI, while the van der Waals force and hydrogen bond played major roles in their binding with BSA. The analysis of synchronous fluorescence, FT-IR and CD spectra showed the change in secondary structure of BSA upon interaction with IPZ, IPZO or IPZI. Site marker competitive experiments indicated that their binding to BSA primarily took place in subdomain IIA. The presence of IPZO and IPZI decreased the quenching constants of IPZ with BSA by about 68.4% and 95.1%, respectively, which possibly resulted from the existence of competitive binding between IPZ and its metabolites with BSA. However, IPZO and IPZI did not change the quenching mechanism of IPZ with BSA, while all the fluorescence quenching was initiated by static quenching procedure combined with non-radiative energy transfer. Our results may have relevant insight into IPZ's bioavailability and efficacy affected by its metabolites. - Highlights: Affinities of IPZ and its metabolites IPZO and IPZI to BSA were investigated. ► Binding of IPZ, IPZO and IPZI to BSA primarily took place in subdomain IIA. ► IPZO and IPZI decreased affinities of IPZ to BSA. ► IPZO and IPZI had competitive binding site with IPZ.

  16. Spectroscopic studies on the interaction of efonidipine with bovine serum albumin

    Directory of Open Access Journals (Sweden)

    N. Wang

    2008-07-01

    Full Text Available Efonidipine hydrochloride is an antihypertensive and antianginal agent with fewer side effects and is better tolerated in the treatment of hypertension with renal impairment. Its interaction with bovine serum albumin (BSA is of great use for the understanding of the pharmacokinetic and pharmacodynamic mechanisms of the drug. The binding of efonidipine to BSA was investigated by fluorescence spectroscopy and circular dichroism. BSA fluorescence was quenched by efonidipine, due to the fact that efonidipine quenched the fluorescence of tryptophan residues mainly by the collision mode. The thermodynamic parameters ΔH0 and ΔS0 were 68.04 kJ/mol and 319.42 J·mol-1·K-1, respectively, indicating that the hydrophobic interactions played a major role. The results of circular dichroism and synchronous fluorescence measurements showed that the binding of efonidipine to BSA led to a conformational change of BSA. The fraction of occupied sites (θ for the 8-anilino-1-naphthalein-sulfonic acid (ANS-BSA system is 85%, whereas for the NZ-105-BSA system, it is 53%, which suggests that the interaction of ANS with BSA is stronger than that of NZ-105 with BSA. Binding studies in the presence of ANS indicated that efonidipine competed with ANS for hydrophobic sites of BSA. The effects of metal ions on the binding constant of the efonidipine-BSA complex were also investigated. The presence of metal ions Zn2+, Mg2+, Al3+, K+, and Ca2+ increased the binding constant of efonidipine_BSA complex, which may prolong the storage period of NZ-105 in blood plasma and enhance its maximum effects.

  17. 4-(Dimethylamino)butyric acid labeling for electrochemiluminescence detection of biological substances by increasing sensitivity with gold nanoparticle amplification.

    Science.gov (United States)

    Yin, Xue-Bo; Qi, Bin; Sun, Xuping; Yang, Xiurong; Wang, Erkang

    2005-06-01

    4-(Dimethylamino)butyric acid (DMBA) labeling combined with gold nanoparticle amplification for electrochemiluminescence (ECL) determination of a biological substance (bovine serum albumin (BSA) and immunoglobulin G (IgG) as models) was presented. After DMBA, an analogue of tripropylamine, was tagged on the (anti)analytes, an ECL signal related to the content of the analytes was generated when the analyte tagged with DMBA was in contact with tris(2,2'-bipyridine)ruthenium (Ru(bpy)(3)2+) solution and a potential was applied. To improve the adsorption capacity, a gold nanoparticle layer was first combined into the surface of the 2-mm-diameter gold electrode. For the determination of BSA, avidin was covalently conjugated to a self-assembled monolayer of 3-mercaptopropanoic acid on the gold nanoparticle layer. Biotinylated BSA-DMBA was then immobilized on the gold nanoparticle layer of the gold electrode via the avidin-biotin reaction. IgG was tested via a typical sandwich-type immobilization method. ECL signals were generated from the electrodes immobilized with BSA or IgG by immersing them in a 1 mmol L-1 Ru(bpy)(3)2+ solution and scanning from 0.5 to 1.3 V versus Ag/AgCl. With gold nanoparticle amplification, the ECL peak intensity was proportional to the concentration over the range 1-80 and 5-100 microg/mL for BSA and IgG consuming 50 microL of sample, respectively. A 10- and 6-fold sensitivity enhancement was obtained for BSA and IgG over their direct immobilization on an electrode using DMBA labeling. The relative standard deviations of five replicate determinations of 10 microg/mL BSA and 20 microg/mL IgG were 8.4 and 10.2%, respectively. High biocompatibility and low cost were the main advantages of the present DMBA labeling technique over the traditional Ru(bpy)(3)2+ labeling. PMID:15924384

  18. Nitrite ion-induced fluorescence quenching of luminescent BSA-Au(25) nanoclusters: mechanism and application.

    Science.gov (United States)

    Unnikrishnan, Binesh; Wei, Shih-Chun; Chiu, Wei-Jane; Cang, Jinshun; Hsu, Pang-Hung; Huang, Chih-Ching

    2014-05-01

    Fluorescence quenching is an interesting phenomenon which is highly useful in developing fluorescence based sensors. A thorough understanding of the fluorescence quenching mechanism is essential to develop efficient sensors. In this work, we investigate different aspects governing the nitrite ion-induced fluorescence quenching of luminescent bovine serum albumin stabilized gold nanoclusters (BSA-Au NCs) and their application for detection of nitrite in urine. The probable events leading to photoluminescence (PL) quenching by nitrite ions were discussed on the basis of the results obtained from ultraviolet-visible (UV-Vis) absorption spectroscopy, X-ray photoelectron spectroscopy (XPS), fluorescence measurements, circular dichroism (CD) spectroscopy, zeta potential and dynamic light scattering (DLS) studies. These studies suggested that PL quenching mainly occurred through the oxidation of Au(0) atoms to Au(i) atoms in the core of BSA-Au NCs mediated by nitrite ions. The interference caused by certain species such as Hg(2+), Cu(2+), CN(-), S(2-), glutathione, cysteine, etc. during the nitrite determination by fluorescence quenching was eliminated by using masking agents and optimising the conditions. Based on these findings we proposed a BSA-Au NC-modified membrane based sensor which would be more convenient for the real life applications such as nitrite detection in urine samples. The BSA-Au NC-modified nitrocellulose membrane (NCM) enabled the detection of nitrite at a level as low as 100 nM in aqueous solutions. This Au NC-based paper probe was validated to exhibit good performance for nitrite analysis in environmental water and urine samples, which makes it useful in practical applications. PMID:24634911

  19. 3-hydroxyflavone-bovine serum albumin interaction in Dextran medium

    Directory of Open Access Journals (Sweden)

    Voicescu Mariana

    2015-01-01

    Full Text Available Spectroscopic analysis of a bioactive flavonol, 3-Hydroxyflavone (3-HF, in systems based on Dextran 70 (Dx70 (an important bio-relevant polysacharide and Bovine Serum Albumin (BSA (a carrier protein, have been studied by fluorescence and circular dichroism. Changes produced by different concentrations of Dx70 on the fluorescent characteristics of 3-HF, and on the excited - state intramolecular proton transfer (ESIPT process were studied. The influence of 3-HF binding and of Dx70 on the secondary structure of BSA were investigated by circular dichroism spectroscopy. The influence of temperature (30-80°C range on the intrinsic Tryptophan fluorescence in 3-HF/BSA/Dx70 systems, was investigated. The results are discussed with relevance to 3-HF as a sensitive fluorescence probe for exploring flavone-protein interaction in plasma expander media and also for its biological evaluation.

  20. Interaction between toxic azo dye C.I. Acid Red 88 and serum albumins

    Energy Technology Data Exchange (ETDEWEB)

    Naveenraj, Selvaraj [Nanomaterials and Solar Energy Conversion Lab, Department of Chemistry, National Institute of Technology, Tiruchirappalli 620015 (India); Solomon, Rajadurai Vijay; Venuvanalingam, Ponnambalam [School of Chemistry, Bharathidasan University, Tiruchirappalli 620024 (India); Asiri, Abdullah M. [The Center of Excellence for Advanced Materials Research, King Abdulaziz University, Jeddah 21413, P.O. Box 80203 (Saudi Arabia); Anandan, Sambandam, E-mail: sanand@nitt.edu [Nanomaterials and Solar Energy Conversion Lab, Department of Chemistry, National Institute of Technology, Tiruchirappalli 620015 (India)

    2013-11-15

    Serum albumin-toxic dye interaction studies will be of paramount importance in the field of toxicology due to its relation towards the distribution and transportation of dye in blood. In this regard, the binding between C.I. Acid Red 88 (AR88) and serum albumins (HSA and BSA) was investigated by using combination of spectroscopic and molecular modeling methods. The fluorescence results revealed that AR88 interact with serum albumins through the combination of static and dynamic quenching mechanism. The distance “r” between serum albumin and AR88 was obtained according to the Forster resonance energy transfer (FRET) theory. Synchronous fluorescence and CD spectral results showed alterations in the microenvironment and conformation of serum albumins. The molecular docking method is also employed to understand the interaction of AR88 with serum albumins. All these studies confirm that BSA has more affinity towards AR88 than that of HSA which suggests that AR88 is more easily transported in the body of bovid than human and so it is more hazardous to bovids. -- Highlights: • AR88 interacts with serum albumin through the combination of both static and dynamic quenching mechanism. • The binding site of AR88 in serum albumins is nearer to tryptophan moiety. • Circular Dichroism spectra showed that AR88 alters α-helicity of serum albumin. • This interaction study could be greatly imperative for further investigations in toxicology.

  1. A combined spectroscopic and molecular docking study on site selective binding interaction of Toluidine blue O with Human and Bovine serum albumins

    International Nuclear Information System (INIS)

    In the present investigation the interaction of a biologically active photodynamic therapeutic agent Toluidine blue O (TBO) with Serum albumins viz Human serum albumin (HSA) and Bovine serum albumin (BSA) was studied using absorption, emission, circular dichroism spectroscopy and molecular docking experiments. The emission titration experiments between HSA/BSA and TBO revealed the existence of strong interactions between TBO and the proteins. The site competitive experiment of HSA and BSA showed that the primary binding site of TBO is located in site I of HSA/BSA involving hydrophobic, hydrogen bonding and electrostatic interaction. To ascertain the results of site competitive experiments, molecular docking was utilized to characterize the binding models of TBO–HSA/BSA complexes. From the molecular docking studies, free energy calculations were undertaken to examine the energy contributions and the role of various amino acid residues of HSA/BSA in TBO binding. The existence of Forster Resonance Energy Transfer (FRET) between the ligand and the protein was utilized to calculate the donor–acceptor distance of TBO and protein. The TBO induced conformational changes of HSA/BSA was established using synchronous emission, three dimensional emission and circular dichroism studies. - Highlights: • Site selective binding interaction of TBO with HSA and BSA were investigated. • TBO quenches the intrinsic fluorescence of HSA/BSA by static quenching process. • Computational studies of TBO with HSA/BSA substantiate the experimental findings. • 3D and CD spectral studies of TBO–HSA/BSA revealed structural changes in protein. • The distance (r) between TBO and HSA/BSA were estimated from FRET theory

  2. Capillary electrophoresis coupled with inductively coupled mass spectrometry as an alternative to cloud point extraction based methods for rapid quantification of silver ions and surface coated silver nanoparticles.

    Science.gov (United States)

    Qu, Haiou; Mudalige, Thilak K; Linder, Sean W

    2016-01-15

    Speciation and accurate quantification of ionic silver and metallic silver nanoparticles are critical to investigate silver toxicity and to determine the shelf-life of products that contain nano silver under various storage conditions. We developed a rapid method for quantification of silver ions and silver nanoparticles using capillary electrophoresis (CE) interfaced with inductively-coupled plasma mass spectrometry (ICPMS). The addition of 2-mercaptopropionylglycine (tiopronin) to the background electrolyte was used to facilitate the chromatographic separation of ionic silver and maintain the oxidation state of silver. The obtained limits of detection were 0.05 μg kg(-1) of silver nanoparticles and 0.03 μg kg(-1) of ionic silver. Nanoparticles of varied sizes (10-110 nm) with different surface coating, including citrate acid, lipoic acid, polyvinylpyrrolidone and bovine serum albumin (BSA) were successfully analyzed. Particularly good recoveries (>93%) were obtained for both ionic silver and silver nanoparticle in the presence of excess amount of BSA. The method was further tested with six commercially available dietary supplements which varied in concentration and matrix components. The summed values of silver ions and silver nanoparticles correlated well with the total silver concentration determined by ICPMS after acid digestion. This method can serve as an alternative to cloud point extraction technique when the extraction efficiency for protein coated nanoparticles is low. PMID:26724893

  3. Albumin microspheres as carriers for the antiarthritic drug celecoxib

    OpenAIRE

    Thakkar, Hetal; Sharma, Rakesh Kumar; Mishra, Anil Kumar; Chuttani, Krishna; Murthy, Rayasa Ramchandra

    2005-01-01

    The present study investigates the preparation of celecoxib-loaded albumin microspheres and the biodistribution of technetium-99m (99mTc)-labeled celecoxib as well as its microspheres after intravenous administration. Microspheres were prepared using a natural polymer BSA using emulsification chemical cross-linking method. The prepared microspheres were characterized for entrapment efficiency, particle size, and in vitro drug release. Surface morphology was studied by scanning electron micros...

  4. Binding of bisphenol A and acrylamide to BSA and DNA: insights into the comparative interactions of harmful chemicals with functional biomacromolecules.

    Science.gov (United States)

    Zhang, Ya-Lei; Zhang, Xian; Fei, Xun-Chang; Wang, Shi-Long; Gao, Hong-Wen

    2010-10-15

    The interactions between bisphenol A (BPA)/acrylamide (AA) and bovine serum albumin (BSA)/deoxyribonucleic acid (DNA) was investigated by the equilibrium dialysis, fluorophotometry, isothermal titration calorimetry (ITC) and circular dichroism (CD). The bindings of BPA and AA to BSA and DNA responded to the partition law and Langmuir isothermal model, respectively. The saturation mole number of AA was calculated to be 24 per mol BSA and 0.26 per mol DNA-P. All the reactions were spontaneous driven by entropy change. BPA stacked into the aromatic hydrocarbon groups of BSA and between adjacent basepairs of DNA via the hydrophobic effect. The interactions of AA with BSA and DNA induced the formation of hydrogen bond and caused changes of their secondary structures. At normal physiological condition, 0.100 mmol/l BPA reduced the binding of vitamin B(2) to BSA by more than 70%, and 2.8 mmol/l AA by almost one half. This work provides an insight into non-covalent intermolecular interaction between organic contaminant and biomolecule, helping to elucidate the toxic mechanism of harmful chemicals. PMID:20673609

  5. Serum albumin binding of structurally diverse neutral organic compounds: data and models.

    Science.gov (United States)

    Endo, Satoshi; Goss, Kai-Uwe

    2011-12-19

    Binding to serum albumin has a strong influence on freely dissolved, unbound concentrations of chemicals in vivo and in vitro. For neutral organic solutes, previous studies have suggested a log-log correlation between the albumin-water partition coefficient and the octanol-water partition coefficient (K(ow)) and postulated highly nonspecific binding that is mechanistically analogous to dissolution into solvents. These relationships and concepts were further explored in this study. Bovine serum albumin (BSA)-water partition coefficients (K(BSA/w)) were measured for 83 structurally diverse neutral organic chemicals in consistent experimental conditions. The correlation between log K(BSA/w) and log K(ow) was moderate, with R(2) = 0.76 and SD = 0.43. The log K(BSA/w) of low-polarity compounds including a series of chlorobenzenes and polycyclic aromatic hydrocarbons increased with log K(ow) linearly up to log K(ow) = 4-5, but then the linear relationship apparently broke off, and the increase became gradual. The fitting of polyparameter linear free energy relationship models with five solute descriptors was just comparable to that of the log K(ow) model (R(2) = 0.78-0.79, SD = 0.41-0.42); the relatively high SD obtained suggests that solvent dissolution models are not capable of modeling albumin binding accurately. A size limitation of the binding site(s) of albumin is suggested as a possible reason for the high SD. An equilibrium distribution model indicates that serum albumin generally has high contributions to the binding in the serum of polar compounds and relatively small low-polarity compounds, whereas albumin binding for large low-polarity compounds is outcompeted by the strong partitioning into lipids due to low relative affinity of albumin for these compounds. PMID:22070391

  6. Mechanism of interaction of vincristine sulphate and rifampicin with bovine serum albumin: A spectroscopic study

    Indian Academy of Sciences (India)

    Bhalchandra P Kamat; Jaldappa Seetharamappa

    2005-11-01

    The mechanism of interaction of vincristine sulphate (VS) and rifampicin (RF) with bovine serum albumin (BSA) has been studied by quenching of BSA fluorescence by RF/VS. The Stern-Volmer plot indicates the presence of a static component in the quenching mechanism. Results also show that both the tryptophan residues of BSA are accessible to VS and RF. The high magnitude of rate constant of quenching indicates that the process of energy transfer occurs by intermolecular interaction and VS/RFbinding site is in close proximity to the tryptophan residues of BSA. Binding studies in the presence of a hydrophobic probe, 8-anilino-1-naphthalene-sulphonic acid sodium salt (ANS) indicate that the VS and RF compete with ANS for hydrophobic sites on the surface of BSA. Small decreases in critical micellar concentrations (CMC) of anionic surfactants in presence of VS/ RF show that the ionic character of VS/RF also contributes to binding. The temperature dependence of the association constant is used to estimate the values of the thermodynamic parameters involved in the interaction of VS/RF with BSA and the results indicate that hydrophobic forces play a significant role in the binding. Circular dichroism studies reveal that the change in helicity of BSA are due to binding of VS/RF to BSA.

  7. Study of the interaction between 5-sulfosalicylic acid and bovine serum albumin by fluorescence spectroscopy

    Energy Technology Data Exchange (ETDEWEB)

    Zhang, Juan, E-mail: zhangjuano13@126.com [Department of Chemistry, School of Basic Medical Sciences, Ningxia Medical University, Yinchuan City, Ningxia Province 750004 (China); Yan, Qianshun; Liu, Jianping; Lu, Xiaohong; Zhu, Yanshu [Department of Chemistry, School of Basic Medical Sciences, Ningxia Medical University, Yinchuan City, Ningxia Province 750004 (China); Wang, Jie; Wang, Shujing [Medical Science Research Center, Ningxia Medical University, Yinchuan City, Ningxia Province 750004 (China)

    2013-02-15

    The interaction between 5-sulfosalicylic acid (SSA) and bovine serum albumin (BSA) at pH 7.40 was studied by fluorescence and UV-vis absorption spectroscopy at different temperatures. The results revealed that SSA caused the fluorescence quenching of BSA through a static quenching procedure. The binding constant K was measured by fluorescence quenching method. The thermodynamic parameters, {Delta}H and {Delta}S, were calculated to be 23.16 kJ mol{sup -1}>0 and 162.37 J mol{sup -1} K{sup -1}>0, respectively, which suggested that the hydrophobic force played a major role in the reaction of SSA on BSA. The distance r between donor (BSA) and acceptor (SSA) was obtained according to the Foerster non-radiation energy transfer theory. The results of synchronous fluorescence spectra, three-dimensional fluorescence spectra and far-UV circular dichroism spectra showed that the interaction between BSA and SSA induced conformational changes in BSA. - Highlights: Black-Right-Pointing-Pointer Interaction of BSA with SSA was investigated by FL, UV-vis and CD spectra. Black-Right-Pointing-Pointer {Delta}H, {Delta}G, {Delta}S, K{sub q}, K{sub sv}, K and r were calculated. Black-Right-Pointing-Pointer Hydrophobic interaction played a major role in the reaction. Black-Right-Pointing-Pointer Conformation of BSA was changed in the presence of SSA.

  8. Study of the interaction between 5-sulfosalicylic acid and bovine serum albumin by fluorescence spectroscopy

    International Nuclear Information System (INIS)

    The interaction between 5-sulfosalicylic acid (SSA) and bovine serum albumin (BSA) at pH 7.40 was studied by fluorescence and UV–vis absorption spectroscopy at different temperatures. The results revealed that SSA caused the fluorescence quenching of BSA through a static quenching procedure. The binding constant K was measured by fluorescence quenching method. The thermodynamic parameters, ΔH and ΔS, were calculated to be 23.16 kJ mol−1>0 and 162.37 J mol−1 K−1>0, respectively, which suggested that the hydrophobic force played a major role in the reaction of SSA on BSA. The distance r between donor (BSA) and acceptor (SSA) was obtained according to the Förster non-radiation energy transfer theory. The results of synchronous fluorescence spectra, three-dimensional fluorescence spectra and far-UV circular dichroism spectra showed that the interaction between BSA and SSA induced conformational changes in BSA. - Highlights: ► Interaction of BSA with SSA was investigated by FL, UV–vis and CD spectra. ► ΔH, ΔG, ΔS, Kq, Ksv, K and r were calculated. ► Hydrophobic interaction played a major role in the reaction. ► Conformation of BSA was changed in the presence of SSA.

  9. Solution combustion synthesis of calcium phosphate particles for controlled release of bovine serum albumin

    International Nuclear Information System (INIS)

    Four different phase compositions of calcium phosphate (CaP) particles were prepared via a solution combustion method. X-ray diffraction (XRD) and Rietveld analysis results revealed that the variations in the nominal Ca/P (molar) ratios were found to provide a favorable control in the different proportions of CaP materials. Bovine serum albumin (BSA) was used as a model protein to study the loading and release behavior. The release profile indicated that the BSA release rates depended on the phase compositions of the CaP particles, and showed an order of TCP-BSA > BCP-1-BSA > BCP-2-BSA > HA-BSA. The results suggested that the BSA protein release rate can be controlled by varying the phase compositions of CaP carriers. Moreover, the release process involved two stages: firstly surface diffusion via ion exchange and secondly intraparticle diffusion. - Highlights: • Solution combustion method was an efficient way to produced CaP powders. • Ca/P (molar) ratios provided a favorable control in the different proportions of phase composition. • BSA release rate varied depending on the phase composition of the CaP particles. • Two kinetic models were chosen to simulate the release kinetics of the drugs from CaP carriers

  10. Solution combustion synthesis of calcium phosphate particles for controlled release of bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Zhao, Junfeng, E-mail: daidai02304@163.com [School of Chemistry and Materials Engineering, Changshu Institute of Technology, Changshu (China); Jiangsu Laboratory of Advanced Functional Materials, Changshu Institute of Technology, Changshu (China); Zhao, Junjie; Qian, Yu; Zhang, Xiali; Zhou, Feifei; Zhang, Hong [School of Chemistry and Materials Engineering, Changshu Institute of Technology, Changshu (China); Lu, Hongbin [National Laboratory of Solid State Microstructures, College of Engineering and Applied Sciences, Nanjing University, Nanjing (China); Chen, JianHua; Wang, XuHong [School of Chemistry and Materials Engineering, Changshu Institute of Technology, Changshu (China); Jiangsu Laboratory of Advanced Functional Materials, Changshu Institute of Technology, Changshu (China); Yu, Wencong [School of Chemistry and Materials Engineering, Changshu Institute of Technology, Changshu (China)

    2015-05-01

    Four different phase compositions of calcium phosphate (CaP) particles were prepared via a solution combustion method. X-ray diffraction (XRD) and Rietveld analysis results revealed that the variations in the nominal Ca/P (molar) ratios were found to provide a favorable control in the different proportions of CaP materials. Bovine serum albumin (BSA) was used as a model protein to study the loading and release behavior. The release profile indicated that the BSA release rates depended on the phase compositions of the CaP particles, and showed an order of TCP-BSA > BCP-1-BSA > BCP-2-BSA > HA-BSA. The results suggested that the BSA protein release rate can be controlled by varying the phase compositions of CaP carriers. Moreover, the release process involved two stages: firstly surface diffusion via ion exchange and secondly intraparticle diffusion. - Highlights: • Solution combustion method was an efficient way to produced CaP powders. • Ca/P (molar) ratios provided a favorable control in the different proportions of phase composition. • BSA release rate varied depending on the phase composition of the CaP particles. • Two kinetic models were chosen to simulate the release kinetics of the drugs from CaP carriers.

  11. Investigation of proton pump inhibitors binding with bovine serum albumin and their relationship to molecular structure

    International Nuclear Information System (INIS)

    The interactions of three proton pump inhibitors (PPIs), omeprazole, pantoprazole and ilaprazole with bovine serum albumin (BSA) have been investigated by fluorescence, synchronous fluorescence, ultraviolet–visible (UV–vis) and circular dichroism (CD). Various binding parameters have been calculated at various temperatures. The results indicated that omeprazole, pantoprazole and ilaprazole had a strong ability to quench the intrinsic fluorescence of BSA with static quenching mechanism, and the binding affinities were significantly affected by different substituents and polarities as the order ilaprazole>pantoprazole>omeprazole. The site marker competitive experiments indicated that the binding of omeprazole, pantoprazole and ilaprazole to BSA primarily took place in subdomain IIA. The results of thermodynamic parameters ΔG, ΔH and ΔS indicated that electrostatic interaction played a major role for PPIs–BSA association. The distance r between PPIs and BSA was evaluated according to the theory of Förster's energy transfer. The quantitative analysis of synchronous fluorescence and CD spectra showed the change in secondary structure of the BSA upon interaction with PPIs by a reduction of α-helix. All the above results many have relevant insight into the PPIs' availability and distribution. - Highlights: ► The interactions of three PPIs with BSA have been investigated. ► The fluorescence quenching mechanism is static quenching. ► Binding affinities were greatly affected by the substituents and polarities. ► The binding of three PPIs to BSA primarily took place in subdomain IIA.

  12. Albumin and multiple sclerosis.

    Science.gov (United States)

    LeVine, Steven M

    2016-01-01

    Leakage of the blood-brain barrier (BBB) is a common pathological feature in multiple sclerosis (MS). Following a breach of the BBB, albumin, the most abundant protein in plasma, gains access to CNS tissue where it is exposed to an inflammatory milieu and tissue damage, e.g., demyelination. Once in the CNS, albumin can participate in protective mechanisms. For example, due to its high concentration and molecular properties, albumin becomes a target for oxidation and nitration reactions. Furthermore, albumin binds metals and heme thereby limiting their ability to produce reactive oxygen and reactive nitrogen species. Albumin also has the potential to worsen disease. Similar to pathogenic processes that occur during epilepsy, extravasated albumin could induce the expression of proinflammatory cytokines and affect the ability of astrocytes to maintain potassium homeostasis thereby possibly making neurons more vulnerable to glutamate exicitotoxicity, which is thought to be a pathogenic mechanism in MS. The albumin quotient, albumin in cerebrospinal fluid (CSF)/albumin in serum, is used as a measure of blood-CSF barrier dysfunction in MS, but it may be inaccurate since albumin levels in the CSF can be influenced by multiple factors including: 1) albumin becomes proteolytically cleaved during disease, 2) extravasated albumin is taken up by macrophages, microglia, and astrocytes, and 3) the location of BBB damage affects the entry of extravasated albumin into ventricular CSF. A discussion of the roles that albumin performs during MS is put forth. PMID:27067000

  13. Albumin microspheres for oral delivery of iron.

    Science.gov (United States)

    Shivakumar, H N; Vaka, Siva Ram Kiran; Murthy, S Narasimha

    2010-01-01

    Bovine serum albumin (BSA) microspheres of ferric pyrophosphate (FPP) intended for passive targeting to the Peyer's patches has been proposed for oral iron supplementation. Microspheres prepared by emulsification chemical cross linking method were characterized for surface topography, entrapment efficiency, particle size, particle charge and in vitro drug release. Microspheres of batch C with FPP to BSA ratio of 1:5 were found to be most suitable for targeting as they exhibited high entrapment (83.88 +/- 4.31), high monodispersity (span = 1.24 +/- 0.01), and least particle size (d(vm) = 4.40 +/- 0.01). In addition the amount of iron retained in these microspheres despite exposure to simulated gastrointestinal conditions for 5 h was found to be 83.72 +/- 4.22%, the highest in the three batches. The in vivo serum iron profiles in normal rats following oral administration displayed a reduced T(max) (2 h), elevated C(max) (106.06 +/- 12.18 mug/dL) and increased AUC (0-16 h) (647.44 +/- 52.33 mug.h/dL) for these microspheres which significantly differed (P <0.05) from FPP solution indicating a higher iron repletion potential of the BSA microspheres. PMID:19635031

  14. Studies on the preparation of T3-BSA, T4-BSA conjugates, and radioimmunoassay use of the produced antisera

    International Nuclear Information System (INIS)

    T3-BSA and T4-BSA conjugates were prepared and identified spectrophotometrically. The Λmax of the conjugates was just coincided with that of BSA, but the molar extinction coefficients of the conjugates were generally larger than that of BSA itself. The molar ratios of T3: BSA and T4: BSA in the prepared conjugates were found to be 9:1 and 5:1, respectively. The titers of the T3 antisera were generally higher (max. 1.5x104:1) than those of T4 (max. 2x103:1), and the average cross reactivity of the T3 antibody with T4 was lower(0.45%)than that of T4 antibody with T3(3approximately4%). The results of the study indicate that the predominant cause of the lower titers and the lower specificity of the T4 antisera comparing with those of T3 is mainly due to the unstability of the T4-BSA and consequent degradation of the conjugate to T3-BSA during preparation, purification, and even during immunization. The lower molar ratio of T4 to BSA in the preparation stage is also considered to be a minor factor. By measuring T3, T4 levels in the reference control serum, it has been confirmed that the prepared antisera can sufficiently be utilized, respectively, in the established radioimmunoassay systems. (Author)

  15. Spectroscopic investigation on sonodynamic and sonocatalytic damage of BSA molecules by Thymol Blue (TB) derivants under ultrasonic irradiation

    Science.gov (United States)

    Wang, Qi; Wu, Qiong; Wang, Jun; Chen, Dandan; Li, Ying; Gao, Jingqun; Wang, Baoxin

    2014-07-01

    In this paper, the Thymol Blue derivants including Thymol Blue (thymolsulfonphthalein), Thymol Blue-DA (3,3‧-Bis [N,N-bis (carboxymethyl) aminomethyl] thymolsulfonphthalein) and Thymol Blue-DA-Fe(III) (3,3‧-Bis [N,N-bis (carboxymethyl) aminomethyl] thymolsulfonphthalein-Ferrous(III)) were adopted as sonosensitizers to study the sonodynamic and sonocatalytic activities under ultrasonic irradiation. At first, the interaction of Thymol Blue derivants with bovine serum albumin (BSA) was studied by fluorescence spectroscopy. On that basis, the sonodynamic and sonocatalytic damages of Thymol Blue derivants to BSA under ultrasonic irradiation were investigated by the combination of UV-vis, circular dichroism (CD) and fluorescence spectroscopy. Meanwhile, some influenced factors (ultrasonic irradiation time, Thymol Blue derivants concentration and ionic strength) on the damaging degree of BSA molecules were also reviewed. In addition, synchronous fluorescence spectra were used to estimate the binding and damage sites of Thymol Blue derivants to BSA. Finally, the generation of ROS during sonodynamic and sonocatalytic processes was confirmed by the method of Oxidation-Extraction Spectrometry (OEP). Perhaps, this paper may offer some important subjects for the study of Thymol Blue derivants in sonodynamic therapy (SDT) and sonocatalytic therapy (SCT) technologies for tumor treatment and the effect of the amino acid and central metal.

  16. Microwave-assisted synthesis of L-glutathione capped ZnSe QDs and its interaction with BSA by spectroscopy

    International Nuclear Information System (INIS)

    Stable, water-soluble and biologically compatible ZnSe quantum dots (QDs) with L-glutathione (GSH) as a capping agent were synthesized in aqueous medium by microwave irradiation. The GSH/Zn/Se molar ratios, reaction temperature, time and pH are the crucial factors for properties of QDs. Fluorescence (FL) spectra, absorption spectra, transmission electron microscopy (TEM), X-ray powder diffraction (XRD) and Fourier transform infrared (FTIR) spectra studies showed that the optical properties of QDs were strong, shape of QDs was similar to spherical and the particle size was about 2–3 nm. The 42% quantum yield (QY) of QDs can be achieved without any post-preparative treatment. The interaction of QDs bioconjugated to bovine serum albumin (BSA) was also studied by absorption and FL spectra experiments. With addition of QDs, the FL intensity of BSA was largely quenched, which can be explained by static mechanism. The results suggested the QDs-BSA binding reaction was a static quenching. -- Highlights: • L-glutathione-capped ZnSe quantum dots were synthesized by microwave assisted in aqueous. • The facile synthesis of ZnSe QDs presented is simple and cost-effective. • Findings suggest the QDs possess highly quantum yield and narrow FWHM without any post-treatment. • The interaction mechanism between QDs and BSA is a static quenching

  17. Characterizing the interaction between oridonin and bovine serum albumin by a hybrid spectroscopic approach

    Energy Technology Data Exchange (ETDEWEB)

    Wang, Zhen [Department of Chemistry, Shantou University, Shantou 515063 (China); Chen, Junhui, E-mail: chenjupush@126.com [Interventional Oncology and Minimally Invasive Therapies Department, Peking University Shenzhen Hospital, Shenzhen 518036 (China); Wang, Shaobin [The Fourth People' s Hospital of Shenzhen, Shenzhen 518033 (China); Chen, Zhanguang, E-mail: kqlu@stu.edu.cn [Department of Chemistry, Shantou University, Shantou 515063 (China)

    2013-02-15

    Oridonin is an effective anticancer drug which has high potency and low systemic toxicity. In this study, the interaction between oridonin and bovine serum albumin (BSA) was investigated by several spectroscopic approaches for the first time. The binding characteristics of oridonin and BSA were determined by fluorescence emission spectra and resonance light scattering spectra. It is showed that the oridonin quenches the fluorescence of BSA and the static quenching constant K{sub SV} is 1.30 Multiplication-Sign 10{sup 4} L mol{sup -1} at 298 K. Moreover, oridonin and BSA form a 1:1 complex with a binding constant of 0.62 Multiplication-Sign 10{sup 4} L mol{sup -1}. On the other hand, the thermodynamic parameters indicate that the binding process was a spontaneous molecular interaction procedure, in which hydrophobic forces played a major role. The structure analysis indicates that oridonin binding results in an increased hydrophobicity around the tryptophan residues of BSA. Additionally, as shown by the UV-vis absorption, synchronous fluorescence and three-dimensional fluorescence results, oridonin could lead to conformational and some microenvironmental changes of BSA. The work provides accurate and full basic data for clarifying the binding mechanism of oridonin with BSA in vitro and is helpful for understanding its effect on protein function during its transportation and distribution in blood. - Highlights: Black-Right-Pointing-Pointer Interaction between oridonin and BSA was evaluated by multi-spectroscopic methods. Black-Right-Pointing-Pointer Binding constant, number of binding sites and thermodynamic parameters were calculated. Black-Right-Pointing-Pointer Oridonin binds to Subdomain II site in BSA and form a 1:1 complex with it. Black-Right-Pointing-Pointer Oridonin-BSA complex is stabilized mainly by hydrophobic force. Black-Right-Pointing-Pointer Oridonin binding induces conformational and microenvironmental changes in BSA.

  18. Probing the binding sites of antibiotic drugs doxorubicin and N-(trifluoroacetyl doxorubicin with human and bovine serum albumins.

    Directory of Open Access Journals (Sweden)

    Daniel Agudelo

    Full Text Available We located the binding sites of doxorubicin (DOX and N-(trifluoroacetyl doxorubicin (FDOX with bovine serum albumin (BSA and human serum albumins (HSA at physiological conditions, using constant protein concentration and various drug contents. FTIR, CD and fluorescence spectroscopic methods as well as molecular modeling were used to analyse drug binding sites, the binding constant and the effect of drug complexation on BSA and HSA stability and conformations. Structural analysis showed that doxorubicin and N-(trifluoroacetyl doxorubicin bind strongly to BSA and HSA via hydrophilic and hydrophobic contacts with overall binding constants of K(DOX-BSA = 7.8 (± 0.7 × 10(3 M(-1, K(FDOX-BSA = 4.8 (± 0.5× 10(3 M(-1 and K(DOX-HSA = 1.1 (± 0.3× 10(4 M(-1, K(FDOX-HSA = 8.3 (± 0.6× 10(3 M(-1. The number of bound drug molecules per protein is 1.5 (DOX-BSA, 1.3 (FDOX-BSA 1.5 (DOX-HSA, 0.9 (FDOX-HSA in these drug-protein complexes. Docking studies showed the participation of several amino acids in drug-protein complexation, which stabilized by H-bonding systems. The order of drug-protein binding is DOX-HSA > FDOX-HSA > DOX-BSA > FDOX>BSA. Drug complexation alters protein conformation by a major reduction of α-helix from 63% (free BSA to 47-44% (drug-complex and 57% (free HSA to 51-40% (drug-complex inducing a partial protein destabilization. Doxorubicin and its derivative can be transported by BSA and HSA in vitro.

  19. Biocompatible capped iron oxide nanoparticles for Vibrio cholerae detection

    Science.gov (United States)

    Sharma, Anshu; Baral, Dinesh; Rawat, Kamla; Solanki, Pratima R.; Bohidar, H. B.

    2015-05-01

    We report the studies relating to fabrication of an efficient immunosensor for Vibrio cholerae detection. Magnetite (iron oxide (Fe3O4)) nanoparticles (NPs) have been synthesized by the co-precipitation method and capped by citric acid (CA). These NPs were electrophoretically deposited onto indium-tin-oxide (ITO)-coated glass substrate and used for immobilization of monoclonal antibodies against Vibrio cholerae (Ab) and bovine serum albumin (BSA) for Vibrio cholerae detection using an electrochemical technique. The structural and morphological studies of Fe3O4 and CA-Fe3O4/ITO were characterized by x-ray diffraction (XRD), transmission electron microscopy (TEM), Fourier transform infrared (FTIR) spectroscopy, and dynamic light scattering (DLS) techniques. The average crystalline size of Fe3O4, CA-Fe3O4 nanoparticles obtained were about 29 ± 1 nm and 37 ± 1 nm, respectively. The hydrodynamic radius of the nanoparticles was found to be 77.35 nm (Fe3O4) and 189.51 nm (CA-Fe3O4) by DLS measurement. The results of electrochemical response studies of the fabricated BSA/Ab/CA-Fe2O3/ITO immunosensor exhibits a good detection range of 12.5-500 ng mL-1 with a low detection limit of 0.32 ng mL-1, sensitivity 0.03 Ω/ng ml-1 cm-2, and reproducibility more than 11 times.

  20. Albumin adsorption on oxide thin films studied by spectroscopic ellipsometry

    Energy Technology Data Exchange (ETDEWEB)

    Silva-Bermudez, P., E-mail: suriel21@yahoo.com [Instituto de Investigaciones en Materiales, Universidad Nacional Autonoma de Mexico, Circuito Exterior s/n, C.U., 04510, Mexico D.F. (Mexico); Unidad de Posgrado, Facultad de Odontologia, Universidad Nacional Autonoma de Mexico, CU, 04510, Mexico D.F. (Mexico); Rodil, S.E.; Muhl, S. [Instituto de Investigaciones en Materiales, Universidad Nacional Autonoma de Mexico, Circuito Exterior s/n, C.U., 04510, Mexico D.F. (Mexico)

    2011-12-15

    Thin films of tantalum, niobium, zirconium and titanium oxides were deposited by reactive magnetron sputtering and their wettability and surface energy, optical properties, roughness, chemical composition and microstructure were characterized using contact angle measurements, spectroscopic ellipsometry, profilometry, X-ray photoelectron spectroscopy and X-ray diffraction, respectively. The purpose of the work was to correlate the surface properties of the films to the Bovine Serum Albumin (BSA) adsorption, as a first step into the development of an initial in vitro test of the films biocompatibility, based on standardized protein adsorption essays. The films were immersed into BSA solutions with different protein concentrations and protein adsorption was monitored in situ by dynamic ellipsometry; the adsorption-rate was dependent on the solution concentration and the immersion time. The overall BSA adsorption was studied in situ using spectroscopic ellipsometry and it was found to be influenced by the wettability of the films; larger BSA adsorption occurred on the more hydrophobic surface, the ZrO{sub 2} film. On the Ta{sub 2}O{sub 5}, Nb{sub 2}O{sub 5} and TiO{sub 2} films, hydrophilic surfaces, the overall BSA adsorption increased with the surface roughness or the polar component of the surface energy.

  1. A subtle calculation method for nanoparticle’s molar extinction coefficient: The gift from discrete protein-nanoparticle system on agarose gel electrophoresis

    Science.gov (United States)

    Zhong, Ruibo; Yuan, Ming; Gao, Haiyang; Bai, Zhijun; Guo, Jun; Zhao, Xinmin; Zhang, Feng

    2016-03-01

    Discrete biomolecule-nanoparticle (NP) conjugates play paramount roles in nanofabrication, in which the key is to get the precise molar extinction coefficient of NPs. By making best use of the gift from a specific separation phenomenon of agarose gel electrophoresis (GE), amphiphilic polymer coated NP with exact number of bovine serum albumin (BSA) proteins can be extracted and further experimentally employed to precisely calculate the molar extinction coefficient of the NPs. This method could further benefit the evaluation and extraction of any other dual-component NP-containing bio-conjugates.

  2. Dye-doped silica-based nanoparticles for bioapplications

    International Nuclear Information System (INIS)

    This paper presents our recent research results on synthesis and bioapplications of dye-doped silica-based nanoparticles. The dye-doped water soluble organically modified silicate (ORMOSIL) nanoparticles (NPs) with the size of 15–100 nm were synthesized by modified Stöber method from methyltriethoxysilane CH3Si(OCH3)3 precursor (MTEOS). Because thousands of fluorescent dye molecules are encapsulated in the silica-based matrix, the dye-doped nanoparticles are extremely bright and photostable. Their surfaces were modified with bovine serum albumin (BSA) and biocompatible chemical reagents. The highly intensive luminescent nanoparticles were combined with specific bacterial and breast cancer antigen antibodies. The antibody-conjugated nanoparticles can identify a variety of bacterium, such as Escherichia coli O157:H7, through antibody–antigen interaction and recognition. A highly sensitive breast cancer cell detection has been achieved with the anti-HER2 monoclonal antibody–nanoparticles complex. These results demonstrate the potential to apply these fluorescent nanoparticles in various biodetection systems. (reviews)

  3. Development of magnetic resonance imaging based detection methods for beta amyloids via sialic acid-functionalized magnetic nanoparticles

    Science.gov (United States)

    Kouyoumdjian, Hovig

    The development of a non-invasive method for the detection of Alzheimer's disease is of high current interest, which can be critical in early diagnosis and in guiding preventive treatment of the disease. The aggregates of beta amyloids are a pathological hallmark of Alzheimer's disease. Carbohydrates such as sialic acid terminated gangliosides have been shown to play significant roles in initiation of amyloid aggregation. Herein, we report a biomimetic approach using sialic acid coated iron oxide superparamagnetic nanoparticles for in vitro detection in addition to the assessment of the in vivo mouse-BBB (Blood brain barrier) crossing of the BSA (bovine serum albumin)-modified ones. The sialic acid functionalized dextran nanoparticles were shown to bind with beta amyloids through several techniques including ELISA (enzyme linked immunosorbent assay), MRI (magnetic resonance imaging), TEM (transmission electron microscopy), gel electrophoresis and tyrosine fluorescence assay. The superparamagnetic nature of the nanoparticles allowed easy detection of the beta amyloids in mouse brains in both in vitro and ex vivo model by magnetic resonance imaging. Furthermore, the sialic acid nanoparticles greatly reduced beta amyloid induced cytotoxicity to SH-SY5Y neuroblastoma cells, highlighting the potential of the glyconanoparticles for detection and imaging of beta amyloids. Sialic acid functionalized BSA (bovine serum albumin) nanoparticles also showed significant binding to beta amyloids, through ELISA and ex vivo mouse brain MRI experiments. Alternatively, the BBB crossing was demonstrated by several techniques such as confocal microscopy, endocytosis, exocytosis assays and were affirmed by nanoparticles transcytosis assays through bEnd.3 endothelial cells. Finally, the BBB crossing was confirmed by analyzing the MRI signal of nanoparticle-injected CD-1 mice.

  4. Cellular distribution of 111In-LDTPA galactose BSA in normal and asialoglycoprotein receptor-deficient mouse liver

    International Nuclear Information System (INIS)

    111In-LDTPA galactose BSA (bovine serum albumin) was used to evaluate the asialoglycoprotein receptor (ASGPR) system in both normal and ASGPR-deficient mice. The radiolabeled glycoprotein had complete liver uptake in both normal and ASGPR-deficient mice. Metabolism and hepatic cell-type distribution studies were performed. The normal mouse excreted greater than 60% of the hepatic activity, while the ASGPR-deficient mouse excreted less than 40% of the hepatic activity. 111In-LDTPA galactose BSA was metabolized to 111In-LDTPA-L-lysine in both mouse types. Normal mice showed 70% of the radioactivity in the hepatocyte, whereas the homozygous ASGPR-deficient mouse had equal activity in the hepatocyte and the hepatic endothelial cell

  5. Prevention of hemodynamic and vascular albumin filtration changes in diabetic rats by aldose reductase inhibitors

    International Nuclear Information System (INIS)

    This study investigated hemodynamic changes in diabetic rats and their relationship to changes in vascular albumin permeation and increased metabolism of glucose to sorbitol. The effects of 6 wk of streptozocin-induced diabetes and three structurally different inhibitors of aldose reductase were examined on (1) regional blood flow (assessed with 15-microns 85Sr-labeled microspheres) and vascular permeation by 125I-labeled bovine serum albumin (BSA) and (2) glomerular filtration rate (assessed by plasma clearance of 57Co-labeled EDTA) and urinary albumin excretion (determined by radial immunodiffusion assay). In diabetic rats, blood flow was significantly increased in ocular tissues (anterior uvea, posterior uvea, retina, and optic nerve), sciatic nerve, kidney, new granulation tissue, cecum, and brain. 125I-BSA permeation was increased in all of these tissues except brain. Glomerular filtration rate and 24-h urinary albumin excretion were increased 2- and 29-fold, respectively, in diabetic rats. All three aldose reductase inhibitors completely prevented or markedly reduced these hemodynamic and vascular filtration changes and increases in tissue sorbitol levels in the anterior uvea, posterior uvea, retina, sciatic nerve, and granulation tissue. These observations indicate that early diabetes-induced hemodynamic changes and increased vascular albumin permeation and urinary albumin excretion are aldose reductase-linked phenomena. Discordant effects of aldose reductase inhibitors on blood flow and vascular albumin permeation in some tissues suggest that increased vascular albumin permeation is not entirely attributable to hemodynamic change

  6. Spectroscopic studies on the interaction between tetrandrine and two serum albumins by chemometrics methods

    Science.gov (United States)

    Cheng, Zhengjun; Liu, Rong; jiang, Xiaohui

    2013-11-01

    The binding interactions of tetrandrine (TETD) with bovine serum albumin (BSA) and human serum albumin (HSA) have been investigated by spectroscopic methods. These experimental data were further analyzed using multivariate curve resolution-alternating least squares (MCR-ALS) method, and the concentration profiles and pure spectra for three species (BSA/HSA, TETD and TETD-BSA/HSA) existed in the interaction procedure, as well as, the apparent equilibrium constants Kapp were evaluated. The binding sites number n and the binding constants K were obtained at various temperatures. The binding distance between TETD and BSA/HSA was 1.455/1.451 nm. The site markers competitive experiments indicated that TETD primarily bound to the tryptophan residue of BSA/HSA within site I. The thermodynamic parameters (ΔG, ΔH and ΔS) calculated on the basis of different temperatures revealed that the binding of TETD-BSA was mainly depended on the hydrophobic interaction strongly and electrostatic interaction, and yet the binding of TETD-HSA was strongly relied on the hydrophobic interaction. The results of synchronous fluorescence, 3D fluorescence and FT-IR spectra show that the conformation of proteins has altered in the presence of TETD. In addition, the effect of some common ions on the binding constants between TETD and proteins were also discussed.

  7. Spectroscopic and molecular modelling studies of binding mechanism of metformin with bovine serum albumin

    Science.gov (United States)

    Sharma, Deepti; Ojha, Himanshu; Pathak, Mallika; Singh, Bhawna; Sharma, Navneet; Singh, Anju; Kakkar, Rita; Sharma, Rakesh K.

    2016-08-01

    Metformin is a biguanide class of drug used for the treatment of diabetes mellitus. It is well known that serum protein-ligand binding interaction significantly influence the biodistribution of a drug. Current study was performed to characterize the binding mechanism of metformin with serum albumin. The binding interaction of the metformin with bovine serum albumin (BSA) was examined using UV-Vis absorption spectroscopy, fluorescence, circular dichroism, density functional theory and molecular docking studies. Absorption spectra and fluorescence emission spectra pointed out the weak binding of metformin with BSA as was apparent from the slight change in absorbance and fluorescence intensity of BSA in presence of metformin. Circular dichroism study implied the significant change in the conformation of BSA upon binding with metformin. Density functional theory calculations showed that metformin has non-planar geometry and has two energy states. The docking studies evidently signified that metformin could bind significantly to the three binding sites in BSA via hydrophobic, hydrogen bonding and electrostatic interactions. The data suggested the existence of non-covalent specific binding interaction in the complexation of metformin with BSA. The present study will certainly contribute to the development of metformin as a therapeutic molecule.

  8. Physicochemical Peculiarities of Iodine-Dimethylsulfoxide-H2O Solutions and Effect on Ion Binding to Bovine Serum Albumin

    OpenAIRE

    Grigoryan, K.; Shilajyan, H.

    2013-01-01

    The interaction of iodine with bovine serum albumin (BSA) in dimethylsulfoxide (DMSO) aqueous solutions was studied by means of fluorescence and UV/Vis absorption spectroscopy methods. Physicochemical peculiarities of these solutions were revealed. The results showed that the tri-iodide ion formed in the 1DMSO : 2H2O solution caused the fluorescence quenching of BSA. The modified Stern-Volmer quenching constant and corresponding thermodynamic parameters, the free energy change ( ), enthalpy c...

  9. Characterization of the Interaction between Bovine Serum Albumin and Lomefloxacin by Capillary Zone Electrophoresis

    Institute of Scientific and Technical Information of China (English)

    Ming GUO; Qing Sen YU; Jian Wei YAN; Fei TAN; Guo Zheng MA

    2004-01-01

    Three capillary zone electrophoresis (CZE) methods of the frontal analysis (FA), vacancy peak (VP) and simplified Hummel-Dreyer (SHD) were applied to investigate interaction between bovine serum albumin (BSA) and lomefloxacin, the experimental condition was established after a large number of tests. Based on the site-binding model, the binding parameters were measured according to the site model by Scatchard.

  10. Interaction of triprolidine hydrochloride with serum albumins: thermodynamic and binding characteristics, and influence of site probes.

    Science.gov (United States)

    Sandhya, B; Hegde, Ashwini H; Kalanur, Shankara S; Katrahalli, Umesha; Seetharamappa, J

    2011-04-01

    The interaction between triprolidine hydrochloride (TRP) to serum albumins viz. bovine serum albumin (BSA) and human serum albumin (HSA) has been studied by spectroscopic methods. The experimental results revealed the static quenching mechanism in the interaction of TRP with protein. The number of binding sites close to unity for both TRP-BSA and TRP-HSA indicated the presence of single class of binding site for the drug in protein. The binding constant values of TRP-BSA and TRP-HSA were observed to be 4.75 ± 0.018 × 10(3) and 2.42 ± 0.024 × 10(4)M(-1) at 294 K, respectively. Thermodynamic parameters indicated that the hydrogen bond and van der Waals forces played the major role in the binding of TRP to proteins. The distance of separation between the serum albumin and TRP was obtained from the Förster's theory of non-radioactive energy transfer. The metal ions viz., K(+), Ca(2+), Co(2+), Cu(2+), Ni(2+), Mn(2+) and Zn(2+) were found to influence the binding of the drug to protein. Displacement experiments indicated the binding of TRP to Sudlow's site I on both BSA and HSA. The CD, 3D fluorescence spectra and FT-IR spectral results revealed the changes in the secondary structure of protein upon interaction with TRP. PMID:21215548

  11. Synthesis of Metal Porphyrins Tailed with Salicylic Acid and their Interaction with Bovine Serum Albumin

    Institute of Scientific and Technical Information of China (English)

    Tao JIA; Kai WANG; Yi Mei ZHAO; Zao Ying LI

    2004-01-01

    A synthetic method of porphyrins tailed with salicylic substituents is described. Reaction of bromoalkoxyphenyl porphyrin 1 with salicylic acid gave porphyrins 2~5. These new compounds were confirmed by 1H NMR, IR, UV-vis, MS and elemental analysis, and observed their interaction with bovine serum albumin (BSA) in fluorescence spectrum.

  12. Binding equilibrium of I~- to serum albumin with resonance Rayleigh scattering

    Institute of Scientific and Technical Information of China (English)

    梁宏; 沈星灿; 蒋治良; 何锡文; 申泮文

    2000-01-01

    The binding equilibrium between l- and human serum albumin (HSA) or bovine serum albumin (BSA) has been studied by means of the resonance Rayleigh scattering (RRS) and equilibrium dialysis. It has been found for the first time that RRS and multiple frequency scattering (MFS) are enhanced as the l- binding to the HSA and BSA, but fluorescence quenches. The equilibrium dialysis results suggest that the binding of l- to HSA and BSA fits a phase-distribution model other than Scsitchard model, and that the order of magnitude of its phase-distribution constant was found to be 104. It is most probable that Cl~ or other anion ions influence the binding of P by changing the ionic strength in the solution. The dialysis at different pH indicates that the binding mechanism is due to the electrostatic forces between the T-and protonated basic amino-acid residues.

  13. Binding equilibrium of I- to serum albumin with resonance Rayleigh scattering

    Institute of Scientific and Technical Information of China (English)

    2000-01-01

    The binding equilibrium between I- and human serum albumin (HSA) or bovine serum albumin (BSA) has been studied by means of the resonance Rayleigh scattering (RRS) and equilibrium dialysis. It has been found for the first time that RRS and multiple frequency scattering (MFS) are enhanced as the I- binding to the HSA and BSA, but fluorescence quenches. The equilibrium dialysis results suggest that the binding of I- to HSA and BSA fits a phase-distribution model other than Scatchard model, and that the order of magnitude of its phase-distribution constant was found to be 104. It is most probable that Cl- or other anion ions influence the binding of I- by changing the ionic strength in the solution. The dialysis at different pH indicates that the binding mechanism is due to the electrostatic forces between the I- and protonated basic amino-acid residues.

  14. Interaction of aconitine with bovine serum albumin and effect of atropine sulphate and glycyrrhizic acid on the binding

    International Nuclear Information System (INIS)

    The interaction of aconitine with bovine serum albumin (BSA) and effect of atropine sulphate and glycyrrhizic acid on binding constant, binding sites, and conformation were studied in an aqueous buffer solution (pH 7.40) by ultraviolet absorption and fluorescence spectroscopy. The study results show that aconitine quenched the endogenous fluorescence of BSA via a dynamic quenching procedure. Predominant intermolecular forces between aconitine and BSA were hydrophobic interactions, which stabilized the complex of aconitine–BSA. The distance between the donor and acceptor was 2.62 nm. The conformation of BSA was investigated by synchronous fluorescence techniques, indicating that the microenvironment around tryptophan (Trp) residues was changed. Furthermore, with the addition of atropine sulphate or glycyrrhizic acid, binding constant and the number of binding sites of aconitine to BSA were decreased, and the conformation had no change, which provide an important theoretical support for aconitine detoxification by atropine sulphate and glycyrrhizic acid. - Highlights: ► Effect of atropine or glycyrrhizic acid on aconitine–BSA binding. ► UV–vis absorption and fluorescence spectroscopic techniques used. ► Aconitine quenched BSA fluorescence via dynamic quenching with r=2.62 nm. ► Atropine sulphate and glycyrrhizic acid decreased KA and n of aconitine–BSA. ► Support for aconitine detoxification by atropine and glycyrrhizic acid.

  15. A study on the binding interaction between the imidazole derivative and bovine serum albumin by fluorescence spectroscopy

    International Nuclear Information System (INIS)

    The interaction between the imidazole derivative 2-(2,4-difluorophenyl)-1-phenyl-1H-imidazo[4,5-f][1,10]phenanthroline (dfppip) and bovine serum albumin (BSA) was investigated by fluorescence and UV–vis absorbance spectroscopy. From the experimental results, it was found that the imidazole derivative has strong ability to quench the intrinsic fluorescence of BSA by forming complexes. Electrostatic interactions play an important role to stabilize the complex. The binding constants and the number of binding sites have been determined in detail. The distance (r) between the donor and the acceptor was obtained according to fluorescence resonance energy transfer (FRET). Conformational changes of BSA were observed from synchronous fluorescence spectroscopy. The effect of metal ions such as Cu2+, Zn2+, Ca2+, Mg2+, Ni2+, Co2+ and Fe2+ on the binding constants between the imidazole derivative and BSA were also studied. - Highlights: ► Interactions between dfppip and BSA were investigated by fluorescence quenching. ► Quenching mechanism mainly arise from the formation of BSA-imidazole complex. ► D→A distance is <8 nm indicates that the energy transfer from BSA to dfppip. ► Synchronous fluorescence spectra to exploit the structural change of BSA. ► Effect of other ions on the binding constants between dfppip and BSA.

  16. Uptake and cytotoxicity of poly(D,L-lactide-co-glycolide) nanoparticles in human colon adenocarcinoma cells

    Energy Technology Data Exchange (ETDEWEB)

    Katsikari, A. [Laboratory of General Microbiology, Department of Genetics, Development and Molecular Biology, School of Biology, Faculty of Sciences and Mathematics, Aristotle University of Thessaloniki, Thessaloniki 54124 (Greece); Patronidou, Chr.; Kiparissides, C. [Section of Analysis, Design and Control of Chemical Processes and Plants, Department of Chemical Engineering, Aristotle University of Thessaloniki, Thessaloniki 54124 (Greece); Arsenakis, M., E-mail: arsenaki@bio.auth.g [Laboratory of General Microbiology, Department of Genetics, Development and Molecular Biology, School of Biology, Faculty of Sciences and Mathematics, Aristotle University of Thessaloniki, Thessaloniki 54124 (Greece)

    2009-12-15

    The main objectives of the present study were to evaluate the cytotoxicity and the mechanisms of uptake of biodegradable lactic acid-glycolic acid copolymer (PLGA) nanoparticle carrier systems in vitro using the human colon adenocarcinoma cell line Caco2. Nanoparticles (NPs) (PLGA 75:25) with an average diameter of 299.5 nm containing bovine serum albumin labeled with fluorescein isothiocyanate (BSA-FITC) as a fluorescent model protein marker were formulated by the double emulsion technique. Various parameters influencing the internalization process by Caco2 cells including concentration of NPs, duration of contact time and cell culture conditions were studied. After overnight exposure of NPs to cells at 37 deg. C, the cell uptake capacity varied in accord with NP concentration, over the 25-800 mug/ml concentration range tested. Maximal uptake of nanoparticles at 37 deg. C occurred at 4 h and was inhibited significantly at 4 deg. C. The extent of NPs internalization was evaluated by confocal laser scanning microscopy. Potential NP toxicity evaluated by modified MTS and lactate dehydrogenase (LDH) colorimetric cytotoxicity tests, measuring mitochondrial activity and membrane integrity respectively, showed that cell viability is significantly reduced at PLGA nanoparticle concentrations greater than 700 mug/ml after 24 and 48 h respectively. The results obtained in vitro for BSA-FITC loaded PLGA nanoparticles underline their potential as carriers for peptide delivery and their utility for the study of NP cell transport and trafficking mechanisms.

  17. Uptake and cytotoxicity of poly(D,L-lactide-co-glycolide) nanoparticles in human colon adenocarcinoma cells

    International Nuclear Information System (INIS)

    The main objectives of the present study were to evaluate the cytotoxicity and the mechanisms of uptake of biodegradable lactic acid-glycolic acid copolymer (PLGA) nanoparticle carrier systems in vitro using the human colon adenocarcinoma cell line Caco2. Nanoparticles (NPs) (PLGA 75:25) with an average diameter of 299.5 nm containing bovine serum albumin labeled with fluorescein isothiocyanate (BSA-FITC) as a fluorescent model protein marker were formulated by the double emulsion technique. Various parameters influencing the internalization process by Caco2 cells including concentration of NPs, duration of contact time and cell culture conditions were studied. After overnight exposure of NPs to cells at 37 deg. C, the cell uptake capacity varied in accord with NP concentration, over the 25-800 μg/ml concentration range tested. Maximal uptake of nanoparticles at 37 deg. C occurred at 4 h and was inhibited significantly at 4 deg. C. The extent of NPs internalization was evaluated by confocal laser scanning microscopy. Potential NP toxicity evaluated by modified MTS and lactate dehydrogenase (LDH) colorimetric cytotoxicity tests, measuring mitochondrial activity and membrane integrity respectively, showed that cell viability is significantly reduced at PLGA nanoparticle concentrations greater than 700 μg/ml after 24 and 48 h respectively. The results obtained in vitro for BSA-FITC loaded PLGA nanoparticles underline their potential as carriers for peptide delivery and their utility for the study of NP cell transport and trafficking mechanisms.

  18. Development of Cy5.5-Labeled Hydrophobically Modified Glycol Chitosan Nanoparticles for Protein Delivery

    Science.gov (United States)

    Chin, Amanda

    , Cy5.5, was used to label the glycol chitosan nanoparticles to enable the noninvasive imaging of living cells. A model protein (bovine serum albumin, BSA) was encapsulated within the glycol chitosan nanoparticles, and its loading efficiency was calculated to be 88%. Release profile of the BSA showed that only 4% (cumulative mass) was achieved by day 7. Minimal cytotoxicity was observed after delivery of the chitosan vehicle alone. To test degradation kinetics, the BSA-loaded nanoparticles were incubated with lysozyme for up to 3 hours and were applied in SDS-PAGE to determine if enzyme-catalyzed degradation triggered premature release of the encapsulated protein. Confocal laser scanning microscopy was used to visualize the spatiotemporal distribution of FITC-BSA-loaded glycol chitosan nanoparticles after delivery to the rat osteosarcoma (ROS17/2.8) and mouse calvaria-derived (MC3T3-E1) cells.

  19. "Smart" nickel oxide based core–shell nanoparticles for combined chemo and photodynamic cancer therapy

    Directory of Open Access Journals (Sweden)

    Bano S

    2016-07-01

    Full Text Available Shazia Bano,1–3,* Samina Nazir,2,* Saeeda Munir,3 Mohamed Fahad AlAjmi,4 Muhammad Afzal,1 Kehkashan Mazhar3 1Department of Physics, The Islamia University of Bahawalpur, 2Nanosciences and Technology Department, National Centre for Physics, Islamabad, 3Institute of Biomedical and Genetic Engineering, Islamabad, Pakistan; 4College of Pharmacy, King Saud University, Riyadh, Kingdom of Saudi Arabia *These authors contributed equally to this work Abstract: We report “smart” nickel oxide nanoparticles (NOPs as multimodal cancer therapy agent. Water-dispersible and light-sensitive NiO core was synthesized with folic acid (FA connected bovine serum albumin (BSA shell on entrapped doxorubicin (DOX. The entrapped drug from NOP-DOX@BSA-FA was released in a sustained way (64 hours, pH=5.5, dark conditions while a robust release was found under red light exposure (in 1/2 hour under λmax=655 nm, 50 mW/cm2, at pH=5.5. The cell viability, thiobarbituric acid reactive substances and diphenylisobenzofuran assays conducted under light and dark conditions revealed a high photodynamic therapy potential of our construct. Furthermore, we found that the combined effect of DOX and NOPs from NOP-DOX@BSA-FA resulted in cell death approximately eightfold high compared to free DOX. We propose that NOP-DOX@BSA-FA is a potential photodynamic therapy agent and a collective drug delivery system for the systemic administration of cancer chemotherapeutics resulting in combination therapy. Keywords: light-triggered drug release, cancer, bovine serum albumin, multi-model therapy

  20. Cost-Benefit Analysis of Nanoparticle Albumin-Bound Paclitaxel versus Solvent-Based Paclitaxel for the Treatment of Metastatic Breast Cancer in the United States

    Science.gov (United States)

    Vichansavakul, Kittaya

    Breast cancer is the second leading cause of death among women in the US. Although early detection and treatment help to increase survival rates, some unfortunate patients develop metastatic breast cancer that has no cure. Palliative treatment is the main objective in this group of patients in order to prolong life and reduce toxicities from interventions. In the advancement of treatment for metastatic breast cancer, solvent-based paclitaxel has been widely used. However, solvent-based paclitaxel often causes adverse reactions. Therefore, researchers have developed a new chemotherapy based on nanotechnology. One of these drugs is the Nanoparticle albumin-bound Paclitaxel. This nanodrug aims to increase therapeutic index by reducing adverse reactions from solvents and to improve efficacy of conventional cytotoxic chemotherapy. Breast cancer is a disease with high epidemiological and economic burden. The treatment of metastatic breast cancer has not only high direct costs but also high indirect costs. Breast cancer affects mass populations, especially women younger than 50 years of age. It relates to high indirect costs due to lost productivity and premature death because the majority of these patients are in the workforce. Because of the high cost of breast cancer therapies and short survival rates, the question is raised whether the costs and benefits are worth paying or not. Due to the rising costs in healthcare and new financing policies that have been developed to address this issue, economic evaluation is an important aspect of the development and use of any new interventions. To guide policy makers on how to allocate limited healthcare resources in the most efficient and effective manner, many economic evaluation methods can be used to measure the costs, benefits, and impacts of healthcare innovations. Currently, economic evaluation and health outcomes studies have focused greatly on cost-effectiveness and cost-utility analysis. However, the previous studies

  1. Co-encapsulation of human serum albumin and superparamagnetic iron oxide in PLGA nanoparticles: Part I. Effect of process variables on the mean size

    Czech Academy of Sciences Publication Activity Database

    Shubhra, Q. T. H.; Kardos, A. F.; Feczkó, T.; Macková, Hana; Horák, Daniel; Tóth, J.; Dósa, G.; Gyenis, J.

    2014-01-01

    Roč. 31, č. 2 (2014), s. 147-155. ISSN 0265-2048 R&D Projects: GA AV ČR(CZ) KAN401220801 Institutional support: RVO:61389013 Keywords : albumin * encapsulation * PLGA (poly d,l-lactic-co-glycolic acid Subject RIV: JB - Sensors, Measurment, Regulation Impact factor: 1.585, year: 2014

  2. Co-encapsulation of human serum albumin and superparamagnetic iron oxide in PLGA nanoparticles: Part II. Effect of process variables on protein model drug encapsulation efficiency

    Czech Academy of Sciences Publication Activity Database

    Shubhra, Q. T. H.; Feczkó, T.; Kardos, A. F.; Tóth, J.; Macková, Hana; Horák, Daniel; Dósa, G.; Gyenis, J.

    2014-01-01

    Roč. 31, č. 2 (2014), s. 156-165. ISSN 0265-2048 R&D Projects: GA AV ČR(CZ) KAN401220801 Institutional support: RVO:61389013 Keywords : encapsulation efficiency * experimental design * human serum albumin Subject RIV: JB - Sensors, Measurment, Regulation Impact factor: 1.585, year: 2014

  3. Using capillary electrophoresis mobility shift assay to study the interaction of CdTe quantum dots with bovine serum albumin

    Institute of Scientific and Technical Information of China (English)

    Li Wen Shao; Chao Qing Dong; Xiang Yi Huang; Ji Cun Ren

    2008-01-01

    In this work, the capillary electrophoresis mobility shift assay (CEMSA) was first adopted to study the interaction of protein with quantum dots (QDs). In this study, bovine serum albumin (BSA) and CdTe QDs were used as model samples. We observed that BSA was facilely adsorbed to CdTe QDs surface, and the QD-BSA complex was formed by a 1:1 stoichiometric ratio. A value of 2.17±0.27×106mol-1 L--1 (at 25℃) for the association constant was obtained by CEMSA.

  4. Comparison of interactions between three food colorants and BSA.

    Science.gov (United States)

    Li, Tian; Cheng, Zhengjun; Cao, Lijun; Jiang, Xiaohui

    2016-03-01

    Fast Green FCF (FCF), Patent Blue V (PBV) and Acid Blue 1 (AB1) are used as food colorants. Multiple spectroscopic techniques were employed to probe in depth the affinity of FCF/PBV/AB1 with BSA in different pH and/or salt concentrations. The results showed that FCF/PBV/AB1 quenched the intrinsic fluorescence of BSA by a static process, and electrostatic force dominated the formation of BSA-FCF/PBV/AB1 complex which was confirmed by the effects of salt on their interactions. Subdomain IIA was the primary binding site for FCF/PBV/AB1 on BSA in the pH range of 5.5-7.4, while both Trp 212 and Trp 134 residues of BSA might be bound by FCF/PBV/AB1 at pH 4.8. The K values suggested that the binding ability of three food colorants with BSA was FCF>PBV>AB1. The results of UV-vis absorption, synchronous fluorescence, 3D fluorescence and FT-IR spectra proved that the structure of BSA altered by FCF/PBV/AB1. PMID:26471614

  5. Investigation of the Interaction between Isoflavonoids and Bovine Serum Albumin by Fluorescence Spectroscopy

    Institute of Scientific and Technical Information of China (English)

    QU,Ling-Bo; CHEN,Xiao-Lan; YANG,Ran; WANG,Ling; ZENG,Hua-Jin

    2007-01-01

    The interactions of bovine serum albumin (BSA) with three structurally related isoflavonoids, genistein, puerarin and daidzein, were studied under physiological conditions by fluorescence spectroscopic technique. The quenching mechanism of these compounds with BSA was suggested as static quenching and the binding constants were determined at different temperatures based on the fluorescence quenching results. The transfer efficiency of energy and distance between the acceptor and BSA were investigated on the basis of the mechanism of the F(o)rster energy transference. According to the thermodynamic parameters it has been suggested that the acting force be mainly hydrophobic force. The comparison of binding potency of the three isoflavonoids to BSA showed that the substitution by 5-OH and 8-Glc could enhance the binding affinity. All these obtained in the work can make us better understand the mode of the action and pharmacological activities of the isoflavonoids.

  6. Competitive Adsorption between Bovine Serum Albumin and Collagen Observed by Atomic Force Microscope

    Institute of Scientific and Technical Information of China (English)

    Yong YU; Pei Qing YING; Gang JIN

    2004-01-01

    Atomic force microscopy (AFM) was used to study the competitive adsorption between bovine serum albumin (BSA) and type Ⅰ collagen on hydrophilic and hydrophobic silicon wafers.BSA showed a grain shape and the type I collagen displayed fibril-like molecules with relatively homogeneous height and width, characterized with clear twisting (helical formation). These AFM images illustrated that quite a lot of type I collagen appeared in the adsorption layer on hydrophilic surface in a competitive adsorption state, but the adsorption of BSA was more preponderant than that of type I collagen on hydrophobic silicon wafer surface. The experiments showed that the influence of BSA on type I collagen adsorption on hydrophilic surface was less than that on hydrophobic surface.

  7. Glycation of bovine serum albumin by ascorbate in vitro: Possible contribution of the ascorbyl radical?

    Science.gov (United States)

    Sadowska-Bartosz, Izabela; Stefaniuk, Ireneusz; Galiniak, Sabina; Bartosz, Grzegorz

    2015-12-01

    Ascorbic acid (AA) has been reported to be both pro-and antiglycating agent. In vitro, mainly proglycating effects of AA have been observed. We studied the glycation of bovine serum albumin (BSA) induced by AA in vitro. BSA glycation was accompanied by oxidative modifications, in agreement with the idea of glycoxidation. Glycation was inhibited by antioxidants including polyphenols and accelerated by 2,​2'-​azobis-​2-​methyl-​propanimidamide and superoxide dismutase. Nitroxides, known to oxidize AA, did not inhibit BSA glycation. A good correlation was observed between the steady-state level of the ascorbyl radical in BSA samples incubated with AA and additives and the extent of glycation. On this basis we propose that ascorbyl radical, in addition to further products of AA oxidation, may initiate protein glycation. PMID:26202868

  8. The investigation of the interaction between NCP-EDA and bovine serum albumin by spectroscopic approaches

    Science.gov (United States)

    Yu, Xianyong; Lu, Shiyu; Yang, Ying; Li, Xiaofang; Yi, Pinggui

    2011-12-01

    The fluorescence and ultraviolet spectroscopies were explored to study the interaction between N-confused porphyrins-edaravone diad (NCP-EDA) and bovine serum albumin (BSA) under simulative physiological condition at different temperatures. The experimental results show that the fluorescence quenching mechanism between NCP-EDA and BSA is a combined quenching (dynamic and static quenching). The binding constants, binding sites and the corresponding thermodynamic parameters (Δ G, Δ H, and Δ S) of the interaction system were calculated at different temperatures. According to Förster non-radiation energy transfer theory, the binding distance between NCP-EDA and BSA was calculated to be 3.63 nm. In addition, the effect of NCP-EDA on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy.

  9. Highly stable, protein capped gold nanoparticles as effective drug delivery vehicles for amino-glycosidic antibiotics

    International Nuclear Information System (INIS)

    A method for the production of highly stable gold nanoparticles (Au NP) was optimized using sodium borohydride as reducing agent and bovine serum albumin as capping agent. The synthesized nanoparticles were characterized using UV–visible spectroscopy, transmission electron microscopy, X‐ray diffraction (XRD) and dynamic light scattering techniques. The formation of gold nanoparticles was confirmed from the appearance of pink colour and an absorption maximum at 532 nm. These protein capped nanoparticles exhibited excellent stability towards pH modification and electrolyte addition. The produced nanoparticles were found to be spherical in shape, nearly monodispersed and with an average particle size of 7.8 ± 1.7 nm. Crystalline nature of the nanoparticles in face centered cubic structure is confirmed from the selected‐area electron diffraction and XRD patterns. The nanoparticles were functionalized with various amino-glycosidic antibiotics for utilizing them as drug delivery vehicles. Using Fourier transform infrared spectroscopy, the possible functional groups of antibiotics bound to the nanoparticle surface have been examined. These drug loaded nanoparticle solutions were tested for their antibacterial activity against Gram-negative and Gram-positive bacterial strains, by well diffusion assay. The antibiotic conjugated Au NP exhibited enhanced antibacterial activity, compared to pure antibiotic at the same concentration. Being protein capped and highly stable, these gold nanoparticles can act as effective carriers for drugs and might have considerable applications in the field of infection prevention and therapeutics. - Highlights: ► Method for NaBH4 reduced and BSA capped gold nanoparticle was standardized. ► Nanoparticles were spherical and nearly monodispersed with a size of 7.8 nm. ► Nanoparticles are extremely stable towards pH modification and electrolyte addition. ► Antibiotic conjugated nanoparticles exhibited enhanced antibacterial activity

  10. Studies of the interaction of CS@ZnS:Mn with bovine serum albumin under illumination

    Energy Technology Data Exchange (ETDEWEB)

    Liu, Li, E-mail: 2476625723@qq.com [Institute of Agricultural Quality Standards and Testing Technology Research, Hubei Academy of Agricultural Science, Wuhan 430064 (China); Xiao, Ling [School of Resource and Environmental Science, Hubei Biomass-Resource Chemistry and Environmental Biotechnology Key Laboratory, Wuhan University, Wuhan 430072 (China)

    2015-09-15

    Highlights: • The interaction and illumination damages of CS@ZnS:Mn D-dots to BSA were studied. • The quenching mechanism of CS@ZnS:Mn D-dots with BSA belongs to dynamic quenching. • The hydrophobic interaction plays a major role; the binding processes are spontaneous. • The FL enhancement of CS@ZnS:Mn D-dots by BSA under UV illumination was observed. • The probable mechanism is mainly a photo-induced free radical procedure. - Abstract: In this study, chitosan coated Mn-doped ZnS quantum dots (CS@ZnS:Mn D-dots) were obtained in aqueous media under ambient pressure. The interaction and illumination damages of CS@ZnS:Mn D-dots with bovine serum albumin (BSA) were studied by means of ultraviolet–visible (UV–vis) and fluorescence (FL) spectra. It was found that the FL of BSA was quenched by CS@ZnS:Mn D-dots. The dominating quenching mechanism of CS@ZnS:Mn D-dots with BSA belongs to dynamic quenching. Hydrophobic interaction plays a major role in the CS@ZnS:Mn–BSA interaction; binding processes are spontaneous. Influencing factors such as illumination time and CS@ZnS:Mn D-dots concentrations were considered. The FL quenching effect of BSA by CS@ZnS:Mn D-dots is enhanced with the increase of illumination time and CS@ZnS:Mn D-dots concentration. The FL enhancement of CS@ZnS:Mn D-dots by BSA under UV illumination was also observed. It was proved that, the interaction of CS@ZnS:Mn D-dots with BSA under UV illumination is mainly a result of a photo-induced free radical procedure. CS@ZnS:Mn D-dots may be used as photosensitizers in photodynamic therapy.

  11. Investigation of three flavonoids binding to bovine serum albumin using molecular fluorescence technique

    International Nuclear Information System (INIS)

    The three flavonoids including naringenin, hesperetin and apigenin binding to bovine serum albumin (BSA) at pH 7.4 was studied by fluorescence quenching, synchronous fluorescence and UV-vis absorption spectroscopic techniques. The results obtained revealed that naringenin, hesperetin and apigenin strongly quenched the intrinsic fluorescence of BSA. The Stern-Volmer curves suggested that these quenching processes were all static quenching processes. At 291 K, the value and the order of the binding constant were KAnaringenin)=4.08x104A(hesperetin)=5.40x104∼KA(apigenin)=5.32x104 L mol-1. The main binding force between the flavonoid and BSA was hydrophobic and electrostatic force. According to the Foerster theory of non-radiation energy transfer, the binding distances (r0) were obtained as 3.36, 3.47 and 3.30 nm for naringenin-BSA, hesperetin-BSA and apigenin-BSA, respectively. The effect of some common ions such as Fe3+, Cu2+, Mg2+, Mn2+, Zn2+ and Ca2+ on the binding was also studied in detail. The competition binding was also performed. The apparent binding constant (K'A) obtained suggested that one flavonoid had an obvious effect on the binding of another flavonoid to protein when they coexisted in BSA solution. - Highlights: → Quenchings of BSA fluorescence by the flavonoids was all static quenchings. → Synchronous fluorescence was applied to study the structural change of BSA. → Binding constant, binding site and binding force were determined. → Competition binding experiments were performed. → One flavonoid had an obvious effect on the binding of another one to BSA.

  12. Investigation of three flavonoids binding to bovine serum albumin using molecular fluorescence technique

    Energy Technology Data Exchange (ETDEWEB)

    Bi Shuyun, E-mail: sy_bi@sina.com [College of Chemistry, Changchun Normal University, Changchun 130032 (China); Yan Lili; Pang Bo; Wang Yu [College of Chemistry, Changchun Normal University, Changchun 130032 (China)

    2012-01-15

    The three flavonoids including naringenin, hesperetin and apigenin binding to bovine serum albumin (BSA) at pH 7.4 was studied by fluorescence quenching, synchronous fluorescence and UV-vis absorption spectroscopic techniques. The results obtained revealed that naringenin, hesperetin and apigenin strongly quenched the intrinsic fluorescence of BSA. The Stern-Volmer curves suggested that these quenching processes were all static quenching processes. At 291 K, the value and the order of the binding constant were K{sub A{sub (naringenin)}}=4.08x10{sup 4}BSA was hydrophobic and electrostatic force. According to the Foerster theory of non-radiation energy transfer, the binding distances (r{sub 0}) were obtained as 3.36, 3.47 and 3.30 nm for naringenin-BSA, hesperetin-BSA and apigenin-BSA, respectively. The effect of some common ions such as Fe{sup 3+}, Cu{sup 2+}, Mg{sup 2+}, Mn{sup 2+}, Zn{sup 2+} and Ca{sup 2+} on the binding was also studied in detail. The competition binding was also performed. The apparent binding constant (K'{sub A}) obtained suggested that one flavonoid had an obvious effect on the binding of another flavonoid to protein when they coexisted in BSA solution. - Highlights: > Quenchings of BSA fluorescence by the flavonoids was all static quenchings. > Synchronous fluorescence was applied to study the structural change of BSA. > Binding constant, binding site and binding force were determined. > Competition binding experiments were performed. > One flavonoid had an obvious effect on the binding of another one to BSA.

  13. Deciphering the binding patterns and conformation changes upon the bovine serum albumin-rosmarinic acid complex.

    Science.gov (United States)

    Peng, Xin; Wang, Xiangchao; Qi, Wei; Huang, Renliang; Su, Rongxin; He, Zhimin

    2015-08-01

    Rosmarinic acid (RA) is an importantly and naturally occurring polyphenol from plants of the mint family with potent biological activities. Here, the in vitro interaction of RA with bovine serum albumin (BSA) has been investigated using various biophysical approaches as well as molecular modeling methods, to ascertain its binding mechanism and conformational changes. The fluorescence results demonstrated that the fluorescence quenching of BSA by RA was mainly the result of the formation of a ground state BSA-RA complex, and BSA had one high affinity RA binding site with a binding constant of 4.18 × 10(4) mol L(-1) at 298 K. Analysis of thermodynamic parameters revealed that hydrophobic and hydrogen bond interactions were the dominant intermolecular force in the complex formation. The primary binding site of RA in BSA (site I) had been identified by site marker competitive experiments. The distance between RA and the tryptophan residue of BSA was evaluated at 3.12 nm based on Förster's theory of non-radiation energy transfer. The UV-vis absorption, synchronous fluorescence, three-dimensional fluorescence, 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence, circular dichroism (CD), and Fourier transform infrared (FT-IR) spectra confirmed that the conformation and structure of BSA were altered in the presence of RA. Moreover, the nuclear magnetic spectroscopy showed that the aromatic groups of RA took part in the binding reaction during the BSA-RA complexation. In addition, the molecular picture of the interaction mechanism between BSA and RA at the atomic level was well examined by molecular docking and dynamics studies. In brief, RA can bind to BSA with noncovalent bonds in a relatively stable way, and these findings will be beneficial to the functional food research of RA. PMID:26146359

  14. Spectroscopic studies on the interaction characteristics between norethisterone and bovine serum albumin

    International Nuclear Information System (INIS)

    The interaction characteristics between norethisterone (NET) and bovine serum albumin (BSA) were studied by fluorescence spectroscopy combined with UV–vis spectrophotometric techniques under simulative physiological conditions. The influence of Cd(II) and/or Se(IV) ions on the interaction between NET and BSA was also investigated. The fluorescence quenching rate constants and binding constants for BSA–NET system were determined at different temperatures. The mechanism of BSA fluorescence quenched by NET was discussed according to the Stern–Volmer equation. The results of thermodynamic parameters, ΔG, ΔS and ΔH, indicated that van der Waals interaction and hydrogen bonding played a major role for NET–BSA association. The results of competitive experiments demonstrated that the primary binding site of NET within subdomain IIA of BSA, and the second binding site within subdomain IIIA. The distance between BSA and NET is estimated to be 3.65 nm based on the Förster resonance energy transfer theory. The conformational change of BSA was observed in the existence of NET, Cd(II) or/and Se(IV) ions by synchronous fluorescence and three-dimensional fluorescence spectra. - Highlights: ► Quenching mechanism of BSA fluorescence by NET was discussed. ► The van der Waals interaction and hydrogen bonding play major roles in the binding. ► Primary binding of NET located at site I in subdomain IIA of BSA. ► Conformational change of BSA in the existence of NET, Cd(II) or/and Se(IV) ions was observed.

  15. Sucrose/bovine serum albumin mediated biomimetic crystallization of calcium carbonate

    Indian Academy of Sciences (India)

    Cheng-Li Yao; Wang-Hua Xu; Ai-Min Ding; Jin-Mao Zhu

    2009-01-01

    To understand the role of the sucrose/bovine serum albumin system in the biomineralization process, we have tested the influence of different concentration of the sucrose/bovine serum albumin (BSA) on calcium carbonate (CaCO3) precipitation. The CaCO3 crystals were characterized by scanning electron microscope (SEM), Fourier transform infrared spectrograph (FT-IR) and powder X-ray diffractometry (XRD). The possible formation mechanism of CaCO3 in the sucrose/bovine serum albumin system was discussed.

  16. PRODUCTION OF CROSS-REACTIVE AUTOANTIBODY BINDING TO BOVINE SERUM ALBUMIN IN THE D-GALACTOSE-INDUCED AGING MOUSE MODEL

    Directory of Open Access Journals (Sweden)

    Ji-Hun Park

    2014-01-01

    Full Text Available The D-galactose (D-gal-induced animal model, generated by repeated subcutaneous D-gal injections over approximately 6 weeks, has been frequently used for diabetes and aging research. However, little research has investigated the direct correlation between D-gal and autoantibody formation despite several reports on diabetes-and aging-related autoantibodies. The purpose of this study was to determine whether repetitive injection of D-gal can induce autoantibody production in mice. First, we used Bovine Serum Albumin (BSA and Advanced Glycation End products (AGE-BSA as the test antigens. The immunoreactivity of serum samples from mice treated with D-gal for 6 weeks was evaluated using Enzyme-Linked Immunosorbent Assay (ELISA. We found that serum samples of D-gal-treated mice had significantly high antibody titers against both BSA and AGE-BSA. Furthermore, the result showed that aminoguanidine treatment, an AGE inhibitor tended to decrease this immunoreactivity. The results of competitive inhibition ELISA using BSA and AGE-BSA as the competitors suggested that the serum samples from D-gal-treated mice contained antibodies not only against BSA but also specific to AGE-BSA. To assess whether the immunoreactivity against BSA is comparable to that against Mouse Serum Albumin (MSA, we examined the reactivity of D-gal-induced antibodies against MSA. Unexpectedly, D-gal-induced antibodies did not react with MSA. This suggests that the production of antibodies by D-gal is in response to an unknown antigen(s, aside from MSA, in mice and that this unknown antigen(s may share similar sequences or three-dimensional structures with BSA.

  17. The synthesis and characterization of monodispersed chitosan-coated Fe3O4 nanoparticles via a facile one-step solvothermal process for adsorption of bovine serum albumin

    OpenAIRE

    Shen, Mao; Yu, Yujing; Fan, Guodong; Chen, Guang; Jin, Ying min; Tang, Wenyuan; Jia, Wenping

    2014-01-01

    Preparation of magnetic nanoparticles coated with chitosan (CS-coated Fe3O4 NPs) in one step by the solvothermal method in the presence of different amounts of added chitosan is reported here. The magnetic property of the obtained magnetic composite nanoparticles was confirmed by X-ray diffraction (XRD) and magnetic measurements (VSM). Scanning electron microscopy (SEM) and transmission electron microscopy (TEM) allowed the identification of spherical nanoparticles with about 150 nm in averag...

  18. Protein-gold clusters-capped mesoporous silica nanoparticles for high drug loading, autonomous gemcitabine/doxorubicin co-delivery, and in-vivo tumor imaging.

    Science.gov (United States)

    Croissant, Jonas G; Zhang, Dingyuan; Alsaiari, Shahad; Lu, Jie; Deng, Lin; Tamanoi, Fuyuhiko; AlMalik, Abdulaziz M; Zink, Jeffrey I; Khashab, Niveen M

    2016-05-10

    Functional nanocarriers capable of transporting high drug contents without premature leakage and to controllably deliver several drugs are needed for better cancer treatments. To address this clinical need, gold cluster bovine serum albumin (AuNC@BSA) nanogates were engineered on mesoporous silica nanoparticles (MSN) for high drug loadings and co-delivery of two different anticancer drugs. The first drug, gemcitabine (GEM, 40wt%), was loaded in positively-charged ammonium-functionalized MSN (MSN-NH3(+)). The second drug, doxorubicin (DOX, 32wt%), was bound with negatively-charged AuNC@BSA electrostatically-attached onto MSN-NH3(+), affording highly loaded pH-responsive MSN-AuNC@BSA nanocarriers. The co-delivery of DOX and GEM was achieved for the first time via an inorganic nanocarrier, possessing a zero-premature leakage behavior as well as drug loading capacities seven times higher than polymersome NPs. Besides, unlike the majority of strategies used to cap the pores of MSN, AuNC@BSA nanogates are biotools and were applied for targeted red nuclear staining and in-vivo tumor imaging. The straightforward non-covalent combination of MSN and gold-protein cluster bioconjugates thus leads to a simple, yet multifunctional nanotheranostic for the next generation of cancer treatments. PMID:27016140

  19. Protein-gold clusters-capped mesoporous silica nanoparticles for high drug loading, autonomous gemcitabine/doxorubicin co-delivery, and in-vivo tumor imaging

    KAUST Repository

    Croissant, Jonas G.

    2016-03-23

    Functional nanocarriers capable of transporting high drug contents without premature leakage and to controllably deliver several drugs are needed for better cancer treatments. To address this clinical need, gold cluster bovine serum albumin (AuNC@BSA) nanogates were engineered on mesoporous silica nanoparticles (MSN) for high drug loadings and co-delivery of two different anticancer drugs. The first drug, gemcitabine (GEM, 40 wt%), was loaded in positively-charged ammonium-functionalized MSN (MSN-NH3+). The second drug, doxorubicin (DOX, 32 wt%), was bound with negatively-charged AuNC@BSA electrostatically-attached onto MSN-NH3+, affording highly loaded pH-responsive MSN-AuNC@BSA nanocarriers. The co-delivery of DOX and GEM was achieved for the first time via an inorganic nanocarrier, possessing a zero-premature leakage behavior as well as drug loading capacities seven times higher than polymersome NPs. Besides, unlike the majority of strategies used to cap the pores of MSN, AuNC@BSA nanogates are biotools and were applied for targeted red nuclear staining and in-vivo tumor imaging. The straightforward non-covalent combination of MSN and gold-protein cluster bioconjugates thus leads to a simple, yet multifunctional nanotheranostic for the next generation of cancer treatments.

  20. Spectroscopy characterization of the interaction between brevifolin carboxylic acid and bovine serum albumin.

    Science.gov (United States)

    Tian, Jianniao; Xie, Yuhuan; Zhao, Yanchun; Li, Caifeng; Zhao, Shulin

    2011-01-01

    Themechanism of binding of the antivirus drug, brevifolin carboxylic acid (BCA) with bovine serum albumin (BSA) was investigated by steady-state and time-resolved fluorescence, circular dichroism (CD), Fourier transform infrared (FT-IR) and Raman spectroscopy under pseudo-physiological conditions for the first time. A strong fluorescence quenching was observed and the quenching mechanism was considered as static quenching. Various binding parameters were evaluated. The quantitative analysis of CD spectral data revealed that the a-helical content of BSA increased from 48.91% (in free BSA) to 52.46% (in bound form) in the presence of BCA. Based on the Förster's theory of non-radiation energy transfer, the relation of the binding average distance r between the donor (BSA) and acceptor (BCA) and acceptor concentration was determined. The changes in association constants of BCA-BSA in the presence of the common ions are also discussed. From the CD, FT-IR, time-resolved fluorescence and Raman spectroscopic results, it is apparent that the interaction of BCA with BSA causes a conformational change in the protein, and the Trp and Tyr residues are buried in more hydrophobic surroundings. BCA mainly binds to residue Trp 212 located in domain II of BSA by hydrophobic interaction and hydrogen bond. PMID:20737652

  1. Urea-induced binding between diclofenac sodium and bovine serum albumin: a spectroscopic insight.

    Science.gov (United States)

    Dohare, Neeraj; Khan, Abbul Bashar; Athar, Fareeda; Thakur, Sonu Chand; Patel, Rajan

    2016-06-01

    We investigated the interaction of diclofenac sodium (Dic.Na) with bovine serum albumin (BSA) in the absence and presence of urea using different spectroscopic techniques. A fluorescence quenching study revealed that the Stern-Volmer quenching constant decreases in the presence of urea, decreasing further at higher urea concentrations. The binding constant and number of binding sites were also evaluated for the BSA-Dic.Na interaction system in the absence and presence of urea using a modified Stern-Volmer equation. The binding constant is greater at high urea concentrations, as shown by the fluorescence results. In addition, for the BSA-Dic.Na interaction system, a static quenching mechanism was observed, which was further confirmed using time-resolved fluorescence spectroscopy. UV-vis spectroscopy provided information about the formation of a complex between BSA and Dic.Na. Circular dichroism was carried out to explain the conformational changes in BSA induced by Dic.Na in the absence and presence of urea. The presence of urea reduced the α-helical content of BSA as the Dic.Na concentration varied. The distance r between the donor (BSA) and acceptor (Dic.Na) was also obtained in the absence and presence of urea, using fluorescence resonance energy transfer. Copyright © 2015 John Wiley & Sons, Ltd. PMID:26564279

  2. Binding interaction of atorvastatin with bovine serum albumin: Spectroscopic methods and molecular docking

    Science.gov (United States)

    Wang, Qi; Huang, Chuan-ren; Jiang, Min; Zhu, Ying-yao; Wang, Jing; Chen, Jun; Shi, Jie-hua

    2016-03-01

    The interaction of atorvastatin with bovine serum albumin (BSA) was investigated using multi-spectroscopic methods and molecular docking technique for providing important insight into further elucidating the store and transport process of atorvastatin in the body and the mechanism of action and pharmacokinetics. The experimental results revealed that the fluorescence quenching mechanism of BSA induced atorvastatin was a combined dynamic and static quenching. The binding constant and number of binding site of atorvastatin with BSA under simulated physiological conditions (pH = 7.4) were 1.41 × 105 M- 1 and about 1 at 310 K, respectively. The values of the enthalpic change (ΔH0), entropic change (ΔS0) and Gibbs free energy (ΔG0) in the binding process of atorvastatin with BSA at 310 K were negative, suggesting that the binding process of atorvastatin and BSA was spontaneous and the main interaction forces were van der Waals force and hydrogen bonding interaction. Moreover, atorvastatin was bound into the subdomain IIA (site I) of BSA, resulting in a slight change of the conformation of BSA.

  3. Binding of anandamide to bovine serum albumin

    DEFF Research Database (Denmark)

    Bojesen, I.N.; Hansen, Harald S.

    2003-01-01

    The endocannabinoid anandamide is of lipid nature and may thus bind to albumin in the vascular system, as do fatty acids. The knowledge of the free water-phase concentration of anandamide is essential for the investigations of its transfer from the binding protein to cellular membranes, because a...... water-phase shuttle of monomers mediates such transfers. We have used our method based upon the use of albumin-filled red cell ghosts as a dispersed biological "reference binder" to measure the water-phase concentrations of anandamide. These concentrations were measured in buffer (pH 7.3) in equilibrium...... data suggest that BSA has one high-affinity binding site for anandamide at all four temperatures. The free energy of anandamide binding (¿G) is calculated to -43.05 kJ mol with a large enthalpy (¿H ) contribution of -42.09 kJ mol. Anandamide has vasodilator activity, and the binding to albumin may...

  4. Novel thermo-sensitive core-shell nanoparticles for targeted paclitaxel delivery

    International Nuclear Information System (INIS)

    Novel thermo-sensitive nanoparticles self-assembled from poly(N,N-diethylacrylamide- co-acrylamide)-block-poly(γ-benzyl L-glutamate) were designed for targeted drug delivery in localized hyperthermia. The lower critical solution temperature (LCST) of nanoparticles was adjusted to a level between physiological body temperature (37 deg. C) and that used in local hyperthermia (about 43 deg. C). The temperature-dependent performances of the core-shell nanoparticles were systemically studied by nuclear magnetic resonance (NMR), circular dichroism (CD), fluorescence spectroscopy, dynamic light scattering (DLS), and atom force microscopy (AFM). The mean diameter of the nanoparticles increased slightly from 110 to 129 nm when paclitaxel (PTX), a poorly water-soluble anti-tumor drug, was encapsulated. A stability study in bovine serum albumin (BSA) solution indicated that the PTX loaded nanoparticles may have a long circulation time under physiological environments as the LCST was above physiological body temperature and the shell remained hydrophilic at 37 deg.C. The PTX release profiles showed thermo-sensitive controlled behavior. The proliferation inhibiting activity of PTX loaded nanoparticles was evaluated against Hela cells in vitro, compared with Taxol (a formulation of paclitaxel dissolved in Cremophor EL and ethanol). The cytotoxicity of PTX loaded nanoparticles increased obviously when hyperthermia was performed. The nanoparticles synthesized here could be an ideal candidate for thermal triggered anti-tumor PTX delivery system.

  5. Fluorescence lifetime measurements of native and glycated human serum albumin and bovine serum albumin

    Science.gov (United States)

    Joshi, Narahari V.; Joshi, Virgina O. d.; Contreras, Silvia; Gil, Herminia; Medina, Honorio; Siemiarczuk, Aleksander

    1999-05-01

    Nonenzymatic glycation, also known as Maillard reaction, plays an important role in the secondary complications of the diabetic pathology and aging, therefore, human serum albumin (HSA) and bovine serum albumin (BSA) were glycated by a conventional method in our laboratory using glucose as the glycating agent. Fluorescence lifetime measurements were carried out with a laser strobe fluorometer equipped with a nitrogen/dye laser and a frequency doubler as a pulsed excitation source. The samples were excited at 295 nm and the emission spectra were recorded at 345 nm. The obtained decay curves were tried for double and triple exponential functions. It has been found that the shorter lifetime increases for glycated proteins as compared with that of the native ones. For example, in the case of glycated BSA the lifetime increased from 1.36 ns to 2.30 ns. Similarly, for HSA, the lifetime increases from 1.58 ns to 2.26 ns. Meanwhile, the longer lifetime changed very slightly for both proteins (from 6.52 ns to 6.72 ns). The increase in the lifetime can be associated with the environmental effect; originated from the attachment of glucose to some lysine residues. A good example is Trp 214 which is in the cage of Lys 225, Lys 212, Lys 233, Lys 205, Lys 500, Lys 199 and Lys 195. If fluorescence lifetime technique is calibrated and properly used it could be employed for assessing glycation of proteins.

  6. Probing the interaction of a new synthesized CdTe quantum dots with human serum albumin and bovine serum albumin by spectroscopic methods.

    Science.gov (United States)

    Bardajee, Ghasem Rezanejade; Hooshyar, Zari

    2016-05-01

    A novel CdTe quantum dots (QDs) were prepared in aqueous phase via a facile method. At first, poly (acrylic amide) grafted onto sodium alginate (PAAm-g-SA) were successfully synthesized and then TGA capped CdTe QDs (CdTe-TGA QDs) were embed into it. The prepared CdTe-PAAm-g-SA QDs were optimized and characterized by transmission electron microscopy (TEM), thermo-gravimetric (TG) analysis, Fourier transform infrared (FT-IR), UV-vis and fluorescence spectroscopy. The characterization results indicated that CdTe-TGA QDs, with particles size of 2.90 nm, were uniformly dispersed on the chains of PAAm-g-SA biopolymer. CdTe-PAAm-g-SA QDs also exhibited excellent UV-vis absorption and high fluorescence intensity. To explore biological behavior of CdTe-PAAm-g-SA QDs, the interactions between CdTe-PAAm-g-SA QDs and human serum albumin (HSA) (or bovine serum albumin (BSA)) were investigated by cyclic voltammetry, FT-IR, UV-vis, and fluorescence spectroscopic. The results confirmed the formation of CdTe-PAAm-g-SA QDs-HSA (or BSA) complex with high binding affinities. The thermodynamic parameters (ΔGCdTe-PAAm-g-SA QDs-HSA (or BSA) complexes. The binding distance between CdTe-PAAm-g-SA QDs and HSA (or BSA)) was calculated about 1.37 nm and 1.27 nm, respectively, according to Forster non-radiative energy transfer theory (FRET). Analyzing FT-IR spectra showed that the formation of QDs-HSA and QDs-BSA complexes led to conformational changes of the HSA and BSA proteins. All these experimental results clarified the effective transportation and elimination of CdTe-PAAm-g-SA QDs in the body by binding to HSA and BSA, which could be a useful guideline for the estimation of QDs as a drug carrier. PMID:26952487

  7. Release of BSA from porous matrices constituted of alginate-Ca2+ and PNIPAAm-interpenetrated networks

    International Nuclear Information System (INIS)

    The synthesis of thermosensitive Interpenetrating Polymer Network (IPN) hydrogels and the release of Bovine Serum Albumin (BSA) from the hydrogels were reported. The hydrogels, constituted of poly(N-isopropyl acrylamide) PNIPAAm network interpenetrated in alginate-Ca2+ network, were synthesized in a two-stepped process. In the first step, PNIPAAm network was synthesized from an aqueous solution containing N-isopropyl acrylamide (NIPAAm) monomers and N,N'-methylene-bis-acrylamide (MBAAm) co-monomers, and sodium alginate (SA) (1 or 2% w/v). The concentration of NIPAAm monomers in the hydrogel-forming solution was always 2.5, 5.0 or 10.0% (w/v). In the second step, alginate-Ca2+ networks were formed by immersion of the membrane, obtained on the first step, in a 1.0% (w/v) aqueous calcium chloride. The IPN hydrogels were characterized as a function of temperature (from 25 to 45 deg. C) through the following measurements: drop water contact angle (DWCA), compression elastic modulus (E) and cross-linking density (νe). The morphology was investigated using scanning electronic microscopy (SEM). In vitro release of BSA from the hydrogels was monitored by UV-Vis spectroscopy at 22 deg. C and 37 deg. C. DWCA results showed a decrease in the hydrogel hydrophilicity when the temperature and/or the PNIPAAm amount on hydrogels were increased. PNIPAAm-loader hydrogels are more compacted and presented elevated rigidity, mainly above 35 deg. C. This trend was attributed to the collapsing of PNIPAAm chains as the hydrogels were warmed above its Lower Critical Solution Temperature (LCST), which in aqueous solution is ca. 32-33 deg. C. The amount of BSA released from the alginate-Ca2+/PNIPAAm hydrogels changes inversely to both amount of PNIPAAm and temperature. The transport of BSA from the hydrogels was evaluated through a conventional model. In the lesser-compacted hydrogels the release occurs mostly by diffusion. In the more compacted ones the chain relaxation contributes to the

  8. Red-blood-cell-like BSA/Zn3(PO4)2 hybrid particles: Preparation and application to adsorption of heavy metal ions

    Science.gov (United States)

    Zhang, Baoliang; Li, Peitao; Zhang, Hepeng; Li, Xiangjie; Tian, Lei; Wang, Hai; Chen, Xin; Ali, Nisar; Ali, Zafar; Zhang, Qiuyu

    2016-03-01

    A novel kind of red-blood-cell-like bovine serum albumin (BSA)/Zn3(PO4)2 hybrid particle is prepared at room temperature by a facile and rapid one-step method based on coordination between BSA and zinc ion. The morphology of the monodisperse hybrid particle shows oblate spheroidal type with a one sided single hole on the surface. The hybrid particle is constructed with BSA/Zn3(PO4)2 nanoplates of 35 nm thick. The average particle size of hybrid particle is 2.3 μm, and its BET specific surface area is 146.64 cm2/g. To clarify the evolution of BSA/Zn3(PO4)2 hybrid particle, SEM and elemental analysis as a function of particle growth time are investigated. The formation mechanism of BSA/Zn3(PO4)2 hybrid particle, which can be described as crystallization, coordination and self-assembly process, is illustrated in detail. The as-prepared BSA/Zn3(PO4)2 hybrid particle is used for adsorption of Cu2+. The hybrid particle displayed excellent adsorption properties on Cu2+. The adsorption efficiency of BSA/Zn3(PO4)2 hybrid particles at 5 min and 30 min are 86.33% and 98.9%, respectively. The maximum adsorption capacity is 6.85 mg/g. Thus, this kind of novel adsorbent shows potential application value in ultra-fast and highly efficient removal of Cu2+.

  9. Quantitation of species differences in albumin–ligand interactions for bovine, human and rat serum albumins using fluorescence spectroscopy: A test case with some Sudlow's site I ligands

    International Nuclear Information System (INIS)

    Albumin, the most abundant plasma protein is an approximately 67 kDa sized water-soluble macromolecule. Since several drugs and xenobiotics circulate in the blood at least partially in albumin-bound form, albumin plays a key role in the pharmacokinetics/toxicokinetics of these chemicals. Most of the drugs and xenobiotics are Sudlow's site I ligands. In numerous studies, bovine serum albumin (BSA) is used for modeling albumin–ligand interactions and the results are extrapolated to human serum albumin (HSA). Furthermore, only limited information is available related to albumin–ligand interactions of different albumin species. Therefore, in our study, we have focused on the quantification of differences between bovine, human and rat serum albumin (RSA) using four Sudlow's site I ligands (luteolin, ochratoxin A, phenylbutazone and warfarin). Interactions were analyzed by fluorescence spectroscopy. Stability constants as well as competing capacities of the ligands were determined, and thermodynamic study was also performed. Our results highlight that there could be major differences between BSA, HSA and RSA in their ligand binding properties. Based on our observations we emphasize that in molecular aspects BSA behaves considerably differently from HSA or from albumins of other species therefore, it is strongly recommended to apply at least some confirmatory measurements when data obtained from other species are attempted to be extrapolated to HSA. -- Highlights: • Albumin–ligand interactions of human, bovine and rat albumins were studied. • Four Sudlow's site I ligands were tested by fluorescence spectroscopy. • Substantial differences were found in stability constants among albumin complexes. • Competing capacity of ligands showed major differences in the studied species. • Data obtained for BSA cannot be directly extrapolated to human albumin

  10. Determination of Conjugation Efficiency of Antibodies and Proteins to the Superparamagnetic Iron Oxide Nanoparticles by Capillary Electrophoresis with Laser-Induced Fluorescence Detection

    International Nuclear Information System (INIS)

    The method based on capillary electrophoresis with laser-induced fluorescence detection (CE/LIF) was developed for determination of magnetic iron oxide nanoparticles (hydrodynamic diameters of 100 nm) functionalized with molecules containing primary amino groups. The magnetic nanoparticles with carboxylic or aminopropyl-trimethoxysilane groups at their surface were conjugated to the model proteins (bovine serum albumin, BSA; streptavidin or goat anti-rabbit immunoglobulin G, IgG) using carbodiimide as a zero-length cross-linker.The nanoparticle-protein conjugates (hydrodynamic diameter 163-194 nm) were derivatized with naphthalene-2,3-dicarboxaldehyde reagent and separated by CE/LIF with a helium-cadmium laser (excitation at 442 nm, emission at 488 nm). The separations were carried out by using a fused-silica capillary (effective length 48 cm, inner diameter 75 um) and 100 mM sodium borate buffer (pH 9.2), the potential was 30 kV. The detection limit for BSA-conjugate was 1.3 pg/10 nl, i.e. about 20 amol. The present method provides an efficient and fast tool for sensitive determination of the efficacy of biomolecular functionalization of magnetic nanoparticles. The CE/LIF technique requires only negligible sample volumes for analysis, which is especially suitable for controlling the process of preparation of functionalized nanoparticles with unique properties aimed to be used for diagnostic or therapeutic purposes

  11. Recognition and binding of β-lactam antibiotics to bovine serum albumin by frontal affinity chromatography in combination with spectroscopy and molecular docking.

    Science.gov (United States)

    Li, Qian; Zhang, Tianlong; Bian, Liujiao

    2016-03-01

    Serum albumins are the most abundant carrier proteins in blood plasma and participate in the binding and transportation of various exogenous and endogenous compounds in the body. This work was designed to investigate the recognition and binding of three typical β-lactam antibiotics including penicillin G (Pen G), penicillin V (Pen V) and cefalexin (Cef) with bovine serum albumin (BSA) by frontal affinity chromatography in combination with UV-vis absorption spectra, fluorescence emission spectra, binding site marker competitive experiment and molecular docking under simulated physiological conditions. The results showed that a BSA only bound with one antibiotic molecule in the binding process, and the binding constants for Pen G-BSA, Pen V-BSA and Cef-BSA complexes were 4.22×10(1), 4.86×10(2) and 3.32×10(3) (L/mol), respectively. All the three β-lactam antibiotics were mainly inserted into the subdomain IIA (binding site 1) of BSA by hydrogen bonds and Van der Waals forces. The binding capacity between the antibiotics and BSA was closely related to the functional groups and flexibility of side chains in antibiotics. This study provided an important insight into the molecular recognition and binding interaction of BSA with β-lactam antibiotics, which may be a useful guideline for the innovative clinical medications and new antibiotic designs with effective pharmacological properties. PMID:26882128

  12. Nanoparticle-cell interactions: molecular structure of the protein corona and cellular outcomes.

    Science.gov (United States)

    Fleischer, Candace C; Payne, Christine K

    2014-08-19

    The use of nanoparticles (NPs) in biology and medicine requires a molecular-level understanding of how NPs interact with cells in a physiological environment. A critical difference between well-controlled in vitro experiments and in vivo applications is the presence of a complex mixture of extracellular proteins. It has been established that extracellular serum proteins present in blood will adsorb onto the surface of NPs, forming a "protein corona". Our goal was to understand how this protein layer affected cellular-level events, including NP binding, internalization, and transport. A combination of microscopy, which provides spatial resolution, and spectroscopy, which provides molecular information, is necessary to probe protein-NP-cell interactions. Initial experiments used a model system composed of polystyrene NPs functionalized with either amine or carboxylate groups to provide a cationic or anionic surface, respectively. Serum proteins adsorb onto the surface of both cationic and anionic NPs, forming a net anionic protein-NP complex. Although these protein-NP complexes have similar diameters and effective surface charges, they show the exact opposite behavior in terms of cellular binding. In the presence of bovine serum albumin (BSA), the cellular binding of BSA-NP complexes formed from cationic NPs is enhanced, whereas the cellular binding of BSA-NP complexes formed from anionic NPs is inhibited. These trends are independent of NP diameter or cell type. Similar results were obtained for anionic quantum dots and colloidal gold nanospheres. Using competition assays, we determined that BSA-NP complexes formed from anionic NPs bind to albumin receptors on the cell surface. BSA-NP complexes formed from cationic NPs are redirected to scavenger receptors. The observation that similar NPs with identical protein corona compositions bind to different cellular receptors suggested that a difference in the structure of the adsorbed protein may be responsible for the

  13. Improved SERS-Active Nanoparticles with Various Shapes for CTC Detection without Enrichment Process with Supersensitivity and High Specificity.

    Science.gov (United States)

    Wu, Xiaoxia; Xia, Yuanzhi; Huang, Youju; Li, Juan; Ruan, Huimin; Chen, Tianxiang; Luo, Liqiang; Shen, Zheyu; Wu, Aiguo

    2016-08-10

    Circulating tumor cells (CTCs) have received more and more attention in medical biology and clinical practice, especially diagnosis, prognosis, and cancer treatment monitoring. The detection of CTCs within the large number of healthy blood cells is a big challenge due to their rarity, which requires a detection method with supersensitivity and high specificity. In this study, we developed three kinds of new nanoparticles with the function of surface-enhanced Raman scattering (SERS) based on spherical gold nanoparticles (AuNPs), gold nanorods (AuNRs), and gold nanostars (AuNSs) with similar particle size, similar modifications, and different shapes for CTC detection without an enrichment process from the blood. The nanoparticles possess strong SERS signal due to modification of 4-mercaptobenzoic acid (4-MBA) (i.e., Raman reporter molecule), possess excellent specificity due to stabilization of reductive bovine serum albumin (rBSA) to reduce the nonspecific catching or uptake by healthy cells in blood, and possess high sensitivity due to conjugation of folic acid (FA) (i.e., a targeted ligand) to identify CTCs. Under the optimized experimental conditions, the results of detection demonstrate that these nanoparticles could all be utilized for CTC detection without enrichment process from the blood with high specificity, and the AuNS-MBA-rBSA-FA is the best one due to its supersensitivity, whose limit of detection (i.e., 1 cell/mL) is much lower than the currently reported lowest value (5 cells/mL). PMID:27434820

  14. Albumin and multiple sclerosis

    OpenAIRE

    LeVine, Steven M

    2016-01-01

    Leakage of the blood–brain barrier (BBB) is a common pathological feature in multiple sclerosis (MS). Following a breach of the BBB, albumin, the most abundant protein in plasma, gains access to CNS tissue where it is exposed to an inflammatory milieu and tissue damage, e.g., demyelination. Once in the CNS, albumin can participate in protective mechanisms. For example, due to its high concentration and molecular properties, albumin becomes a target for oxidation and nitration reactions. Furth...

  15. Triazolopyridyl ketones as a novel class of antileishmanial agents. DNA binding and BSA interaction.

    Science.gov (United States)

    Adam, Rosa; Bilbao-Ramos, Pablo; López-Molina, Sonia; Abarca, Belén; Ballesteros, Rafael; González-Rosende, M Eugenia; Dea-Ayuela, M Auxiliadora; Alzuet-Piña, Gloria

    2014-08-01

    A new series of triazolopyridyl pyridyl ketones has been synthetized by regioselective lithiation of the corresponding [1,2,3]triazolo[1,5-a]pyridine at 7 position followed by reaction with different electrophiles. The in vitro antileishmanial activity of these compounds was evaluated against Leishmaniainfantum, Leishmaniabraziliensis, Leishmaniaguyanensis and Leishmaniaamazonensis. Compounds 6 and 7 were found to be the most active leishmanicidal agents. Both of them showed activities at micromolar concentration against cultured promastigotes of Leishmania spp. (IC₅₀=99.8-26.8 μM), without cytotoxicity on J774 macrophage cells. These two compounds were also tested in vivo in a murine model of acute infection by L. infantum. The triazolopyridine derivative 6 was effective against both spleen and liver parasites forms, while 7 was inactive against liver parasites. Mechanistic aspects of the antileishmanial activity were investigated by means of DNA binding studies (UV-titration and viscosimetry). Results have revealed that these active ligands are able to interact strongly with DNA [Kb=1.14 × 10(5)M(-1) (6) and 3.26 × 10(5)M(-1) (7)]. Moreover, a DNA groove binding has been proposed for both 6 and 7. To provide more insight on the mode of action of compounds 6 and 7 under biological conditions, their interaction with bovine serum albumin (BSA) was monitored by fluorescence titrations and UV-visible spectroscopy. The quenching constants and binding parameters were determined. Triazolopyridine ketones 6 and 7 have exhibited significant affinity towards BSA [Kb=2.5 × 10(4)M(-1) (6) and 1.9 × 10(4)M(-1) (7)]. Finally, to identify the binding location of compounds 6 and 7 on the BSA, competitive binding experiments were carried out, using warfarin, a characteristic marker for site I, and ibuprofen as one for site II. Results derived from these studies have indicated that both compounds interact at BSA site I and, to a lesser extent, at site II. PMID:24953952

  16. Interaction of malachite green with bovine serum albumin: Determination of the binding mechanism and binding site by spectroscopic methods

    International Nuclear Information System (INIS)

    The interaction between malachite green (MG) and bovine serum albumin (BSA) under simulative physiological conditions was investigated by the methods of fluorescence spectroscopy, UV-vis absorption and circular dichroism (CD) spectroscopy. Fluorescence data showed that the fluorescence quenching of BSA by MG was the result of the formation of the MG-BSA complex. According to the modified Stern-Volmer equation, the effective quenching constants (Ka) between MG and BSA at four different temperatures were obtained to be 3.734 x 104, 3.264 x 104, 2.718 x 104, and 2.164 x 104 L mol-1, respectively. The enthalpy change (ΔH) and entropy change (ΔS) were calculated to be -27.25 kJ mol-1 and -11.23 J mol-1 K-1, indicating that van der Waals force and hydrogen bonds were the dominant intermolecular force in stabilizing the complex. Site marker competitive experiments indicated that the binding of MG to BSA primarily took place in sub-domain IIA. The binding distance (r) between MG and the tryptophan residue of BSA was obtained to be 4.79 nm according to Foerster theory of non-radioactive energy transfer. The conformational investigation showed that the presence of MG decreased the α-helical content of BSA (from 62.6% to 55.6%) and induced the slight unfolding of the polypeptides of protein, which confirmed some micro-environmental and conformational changes of BSA molecules

  17. Albumin adsorption on CoCrMo alloy surfaces

    Science.gov (United States)

    Yan, Yu; Yang, Hongjuan; Su, Yanjing; Qiao, Lijie

    2015-12-01

    Proteins can adsorb on the surface of artificial joints immediately after being implanted. Although research studying protein adsorption on medical material surfaces has been carried out, the mechanism of the proteins’ adsorption which affects the corrosion behaviour of such materials still lacks in situ observation at the micro level. The adsorption of bovine serum albumin (BSA) on CoCrMo alloy surfaces was studied in situ by AFM and SKPFM as a function of pH and the charge of CoCrMo alloy surfaces. Results showed that when the specimens were uncharged, hydrophobic interaction could govern the process of the adsorption rather than electrostatic interaction, and BSA molecules tended to adsorb on the surfaces forming a monolayer in the side-on model. Results also showed that adsorbed BSA molecules could promote the corrosion process for CoCrMo alloys. When the surface was positively charged, the electrostatic interaction played a leading role in the adsorption process. The maximum adsorption occurred at the isoelectric point (pH 4.7) of BSA.

  18. Kinetic studies of bovine serum albumin interaction with PG and TBHQ using surface plasmon resonance.

    Science.gov (United States)

    Fathi, Farzaneh; Ezzati Nazhad Dolatanbadi, Jafar; Rashidi, Mohammad-Reza; Omidi, Yadollah

    2016-10-01

    Propyl gallate (PG) and tert-butylhydroquinone (TBHQ) are examples of phenolic antioxidant agents, which have widespread uses in food industry. In this study, for the first time, we report on the interaction of PG and TBHQ with bovine serum albumin (BSA) using surface plasmon resonance (SPR). In order to modify Au slide with carboxyl functional group, 11-mercaptoundecanoic acid (MUA) was used. After activation of carboxylic groups, BSA was immobilized onto the MUA through both covalent amide bond and electrostatic binding formation. The SPR analysis showed dose-response sensograms of BSA upon increasing concentration of PG and TBHQ. At pH 4.5, the equilibrium dissociation constant or affinity unit (KD) for PG and TBHQ were 1.89e(-10) and 1.49e(-10) and at pH 7.5 were 4.74e(-10) and 1.83e(-9), respectively. The smaller amount of KD demonstrated high food additive molecules affinity to BSA. Based on these findings, it can be concluded that PG and TBHQ molecules can interact with BSA and effectively distributed within the body. Besides, SPR can be considered as useful automatic tool for quantification of PG and TBHQ interaction with serum albumin and it can deliver precise real-time kinetic data. PMID:27327906

  19. Effect of bovine serum albumin on the functionality and structure of catanionic surfactant at air–buffer interface

    International Nuclear Information System (INIS)

    Interaction of bovine serum albumin (BSA) with the solvent spread monolayer of a catanionic surfactant, octadecyltrimethylammonium dodecylsulfate, (C18TA+DS−) at the air–buffer interface was investigated by measuring the surface pressure with time and change in surface area. Dipalmitoylphosphatidylcholine (DPPC) was used as reference. Kinetics of BSA desorption from the interface to the buffer subphase, that of C18TA+DS− and DPPC through their interaction with BSA, were also studied at different BSA concentrations (in the subphase) and surface pressures. Surface pressure (π)–area (A) isotherms (at pH = 5.4, μ = 0.01, T = 298 K) revealed that the coacervate/DPPC monolayer becomes expanded in the presence of BSA at low π while their protein bound species are released into the subphase at high π. Film morphology, studied by epifluorescence microscopy (EFM) and atomic force microscopy (AFM), reveals that the sizes of the domains of both DPPC and coacervate decrease in the presence of BSA. Presence of BSA in the coacervate and DPPC monolayer was supported from AFM data analysis. Highlights: ► Effect of BSA on the functionality and structure of C18TA+DS−/DPPC at the air–buffer interface was studied. ► BSA molecules coadsorb at lower surface pressure, while they abstract amphiphiles at higher surface pressure into the bulk. ► Kinetic studies of adsorption/desorption of BSA at/from the interface were performed. ► Organized amphiphiles are perturbed in the presence of BSA.

  20. Corrosion behaviour of niobium in phosphate buffered saline solutions with different concentrations of bovine serum albumin

    International Nuclear Information System (INIS)

    Highlights: ► Corrosion of Nb was investigated in phosphate buffered saline solutions. ► Addition of bovine serum albumin lowered the open circuit potential of Nb. ► Open circuit potential, polarization resistance and impedance increased with time. ► Bovine serum albumin molecules and PO43− competitively adsorbed on Nb surface. ► A surface distribution of time-constants was proposed. - Abstract: The corrosion behaviour of Nb was studied in phosphate buffered saline (PBS) solutions at a presence of 0–6 g L−1 bovine serum albumin (BSA). Addition of BSA to PBS solutions lowered the open circuit potential (OCP). OCP, polarization resistance and impedance increased over immersion time. The adsorption process of BSA on Nb surface was found to be faster than that of the PO43−. According to X-ray Photoelectron Spectroscopy (XPS) a competitive adsorption between PO43− and BSA was in effect during the immersion process. Based on the analysis of effective capacitances, a surface distribution of time-constants was proposed.

  1. Cationized bovine serum albumin as gene carrier: Influence of specific secondary structure on DNA complexibility and gene transfection.

    Science.gov (United States)

    Du, Jianwei; Li, Bangbang; Zhang, Peng; Wang, Youxiang

    2016-07-01

    In this research, BSA, one of the natural rigid globular proteins with ca. 51% of α-helix secondary structure, was utilized to prepare cationized BSA (cBSA) as gene carrier. Tetraethylenepentamine (TEPA) or polyethylenimine (PEI1800) was grafted to BSA with different grafting levels. Based on the circular dichoism (CD) spectra, all cBSA remained α-helical structure to some degree. This was exciting to endow cBSA with quite different DNA complexibility and cellular biology behavior from the random coiled and flexible polycations such as PEI and poly-l-lysine (PLL). Strangely, the DNA condensability decreased with the increment of TEPA or PEI1800 grafting level. Also, the cBSA could condense DNA effectively to form irregular nanoparticles around 50-200nm above N/P ratio of 10. On account of the excellent hydration of BSA, the cBSA/DNA complexes revealed good colloidal stability under physiological salt condition. Cell culture experiments indicated this BSA-based gene carrier possessed good cellular compatibility. Surprisingly, cBSA/DNA complexes could be uptaken excellently by up to 90% cells. This might be owing to the agitation effect of α-helical structure and the positive potential of these complexes. BSA-PEI1800/DNA complexes with quick endosome escape even had transfection efficiency as high as PEI25k/DNA complexes. Overall, this paper provided us the potential of cBSA as gene carrier and might have some instructions in the design of protein-based gene delivery system. PMID:26998865

  2. Study of the interaction of gemini surfactant NAE12-4-12 with bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Tu Sheng [Chemical Synthesis and Pollution Control Key Laboratory of Sichuan Province, China West Normal University, Nanchong, Sichuan 673002 (China); Jiang Xiaohui, E-mail: jxh2314508@163.com [Chemical Synthesis and Pollution Control Key Laboratory of Sichuan Province, China West Normal University, Nanchong, Sichuan 673002 (China); Zhou Limei; Yin Wenmin; Wang Houchen [Chemical Synthesis and Pollution Control Key Laboratory of Sichuan Province, China West Normal University, Nanchong, Sichuan 673002 (China); Duan Ming; Liu Pingli [State Key Laboratory of Oil and Gas Reservoir Geology and Exploitation, Southwest Petroleum University, Chengdu, Sichuan 610500 (China); Jiang Xiaomin [Southwest Electric Power Design Institute, Chengdu, Sichuan 610021 (China)

    2012-02-15

    The interaction of 1,4-bis(3-(dodecyloxylacyl)pyridinium)butane dibromide (designated as NAE12-4-12) and bovine serum albumin (BSA) was investigated by UV-vis absorption, FTIR and fluorescence spectroscopies. The results showed that NAE12-4-12 had strong ability to quench the intrinsic fluorescence of BSA and caused the emission peak blueshift through a static quenching process. The binding constant of NAE12-4-12 with BSA decreased with increasing temperature. The binding process was exothermic, spontaneous and enthalpy driven. The distance between BSA and NAE12-4-12 decreased with incremental concentration of NAE12-4-12. Furthermore, FTIR spectra of BSA-NAE12-4-12 reflected that the secondary structure of BSA changed in the presence of NAE12-4-12, and the curve fitting of IR spectra revealed that the content of {alpha}-helix decreased while those of {beta}-sheet, {beta}-turn and random coil rose. - Highlights: Black-Right-Pointing-Pointer NAE12-4-12 is a newly synthesized cationic gemini surfactant. Black-Right-Pointing-Pointer It effectively reduces intrinsic fluorescence of BSA through static quenching. Black-Right-Pointing-Pointer Binding constant of NAE12-4-12-BSA decreases with rising temperature. Black-Right-Pointing-Pointer Distance between BSA and NAE12-4-12 diminishes with NAE12-4-12 concentration. Black-Right-Pointing-Pointer Content of {alpha}-helix of BAS decreases while those of other structures rise up.

  3. Protections of bovine serum albumin protein from damage on functionalized graphene-based electrodes by flavonoids.

    Science.gov (United States)

    Sun, Bolu; Gou, Yuqiang; Xue, Zhiyuan; Zheng, Xiaoping; Ma, Yuling; Hu, Fangdi; Zhao, Wanghong

    2016-05-01

    A sensitive electrochemical sensor based on bovine serum albumin (BSA)/poly (diallyldimethylammonium chloride) (PDDA) functionalized graphene nanosheets (PDDA-G) composite film modified glassy carbon electrode (BSA/PDDA-G/GCE) had been developed to investigate the oxidative protein damage and protections of protein from damage by flavonoids. The performance of this sensor was remarkably improved due to excellent electrical conductivity, strong adsorptive ability, and large effective surface area of PDDA-G. The BSA/PDDA-G/GCE displayed the greatest degree of BSA oxidation damage at 40min incubation time and in the pH5.0 Fenton reagent system (12.5mM FeSO4, 50mM H2O2). The antioxidant activities of four flavonoids had been compared by fabricated sensor based on the relative peak current ratio of SWV, because flavonoids prevented BSA damage caused by Fenton reagent and affected the BSA signal in a solution containing Co(bpy)3(3+). The sensor was characterized by cyclic voltammetry (CV), electrochemical impedance spectroscopy (EIS), and scanning electron microscopy (SEM). UV-vis spectrophotometry and FTIR were also used to investigate the generation of hydroxyl radical and BSA damage, respectively. On the basis of results from electrochemical methods, the order of the antioxidant activities of flavonoids is as follows: (+)-catechin>kaempferol>apigenin>naringenin. A novel, direct SWV analytical method for detection of BSA damage and assessment of the antioxidant activities of four flavonoids was developed and this electrochemical method provided a simple, inexpensive and rapid detection of BSA damage and evaluation of the antioxidant activities of samples. PMID:26952415

  4. Effects of urea, metal ions and surfactants on the binding of baicalein with bovine serum albumin

    Directory of Open Access Journals (Sweden)

    Atanu Singha Roy

    2016-08-01

    Full Text Available The interaction of baicalein with bovine serum albumin (BSA was investigated with the help of spectroscopic and molecular docking studies. The binding affinity of baicalein towards BSA was estimated to be in order of 105 M−1 from fluorescence quenching studies. Negative ΔH° (−5.66±0.14 kJ/mol and positive (ΔS° (+79.96±0.65 J/mol K indicate the presence of electrostatic interactions along with the hydrophobic forces that result in a positive ΔS°. The hydrophobic association of baicalein with BSA diminishes in the presence of sodium dodecyl sulfate (SDS due to probable hydrophobic association of baicalein with SDS, resulting in a negative ΔS° (−40.65±0.87 J/mol K. Matrix-assisted laser desorption ionization/time of flight (MALDI--TOF experiments indicate a 1:1 complexation between baicalein and BSA. The unfolding and refolding phenomena of BSA were investigated in the absence and presence of baicalein using steady-state and fluorescence lifetime measurements. It was observed that the presence of urea ruptured the non-covalent interaction between baicalein and BSA. The presence of metal ions (Ag+, Mg2+, Ni2+, Mn2+, Co2+and Zn2+ increased the binding affinity of ligand towards BSA. The changes in conformational aspects of BSA after ligand binding were also investigated using circular dichroism (CD and Fourier transform infrared (FT-IR spectroscopic techniques. Site selectivity studies following molecular docking analyses indicated the binding of baicalein to site 1 (subdomain IIA of BSA.

  5. Preparation, characterization, and safety evaluation of poly(lactide-co-glycolide) nanoparticles for protein delivery into macrophages.

    Science.gov (United States)

    Guedj, Anne-Sophie; Kell, Arnold J; Barnes, Michael; Stals, Sandra; Gonçalves, David; Girard, Denis; Lavigne, Carole

    2015-01-01

    Following infection, HIV establishes reservoirs within tissues that are inaccessible to optimal levels of antiviral drugs or within cells where HIV lies latent, thus escaping the action of anti-HIV drugs. Macrophages are a persistent reservoir for HIV and may contribute to the rebound viremia observed after antiretroviral treatment is stopped. In this study, we further investigate the potential of poly(lactic-co-glycolic) acid (PLGA)-based nanocarriers as a new strategy to enhance penetration of therapeutic molecules into macrophages. We have prepared stable PLGA nanoparticles (NPs) and evaluated their capacity to transport an active molecule into the human monocyte/macrophage cell line THP-1 using bovine serum albumin (BSA) as a proof-of-concept compound. Intracellular localization of fluorescent BSA molecules encapsulated into PLGA NPs was monitored in live cells using confocal microscopy, and cellular uptake was quantified by flow cytometry. In vitro and in vivo toxicological studies were performed to further determine the safety profile of PLGA NPs including inflammatory effects. The size of the PLGA NPs carrying BSA (PLGA-BSA) in culture medium containing 10% serum was ~126 nm in diameter, and they were negatively charged at their surface (zeta potential =-5.6 mV). Our confocal microscopy studies and flow cytometry data showed that these PLGA-BSA NPs are rapidly and efficiently taken up by THP-1 monocyte-derived macrophages (MDMs) at low doses. We found that PLGA-BSA NPs increased cellular uptake and internalization of the protein in vitro. PLGA NPs were not cytotoxic for THP-1 MDM cells, did not modulate neutrophil apoptosis in vitro, and did not show inflammatory effect in vivo in the murine air pouch model of acute inflammation. In contrast to BSA alone, BSA encapsulated into PLGA NPs increased leukocyte infiltration in vivo, suggesting the in vivo enhanced delivery and protection of the protein by the polymer nanocarrier. We demonstrated that PLGA

  6. Study on the conjugation mechanism of colistin sulfate with bovine serum albumin and effect of the metal ions on the reaction

    International Nuclear Information System (INIS)

    Colistin sulfate (CS) can quench the fluorescence of bovine serum albumin (BSA) in an aqueous solution at pH 7.40. The static fluorescence-quenching process between BSA and CS was confirmed and the binding constant, the number of binding sites and thermodynamic data for the interaction between BSA and CS were also obtained. Results showed that the order of magnitude of binding constant (Ka) was 104, and the number of binding site (n) in the binary system was approximately equal to 1; electrostatic force played an important role on the conjugation reaction between BSA and CS. On the basis of the Förster theory of the resonance energy transfer, the binding distance (r) between CS and BSA was less than 7 nm. Comparing the quenching of protein fluorescence excited at 280 nm and 295 nm and from the site marker replacement experiments, it was shown that the primary CS binding site was located in the sub-domain IIA (site I) of BSA. Synchronous fluorescence spectra clearly revealed that the binding of CS with BSA can induce conformation changes in BSA. In addition, the effects of common metal ions on the binding constants of CS–BSA complex were also discussed. It was shown that, except Cu2+, the high metal ion concentrations improved the CS efficacy. - Highlights: ► Complex formation is dominant for the reduction of BSA fluorescence. ► Primary binding site for drug is located in the sub-domain IIA of BSA. ► Electrostatic force played a main role between the drug and the BSA. ► The BSA structure changes upon drug complexation. ► Higher concentrations of metal ions have good effects to improve efficacy of drug except Cu2+.

  7. Study on the conjugation mechanism of colistin sulfate with bovine serum albumin and effect of the metal ions on the reaction

    Energy Technology Data Exchange (ETDEWEB)

    Liu Baosheng, E-mail: lbs@hbu.edu.cn [Key Laboratory of Medical Chemistry and Molecular Diagnosis, Ministry of Education, College of Chemistry and Environmental Science, Hebei University, Baoding 071002 (China); Yang Chao; Yan Xiaona; Wang Jing; Lv Yunkai [Key Laboratory of Medical Chemistry and Molecular Diagnosis, Ministry of Education, College of Chemistry and Environmental Science, Hebei University, Baoding 071002 (China)

    2012-05-15

    Colistin sulfate (CS) can quench the fluorescence of bovine serum albumin (BSA) in an aqueous solution at pH 7.40. The static fluorescence-quenching process between BSA and CS was confirmed and the binding constant, the number of binding sites and thermodynamic data for the interaction between BSA and CS were also obtained. Results showed that the order of magnitude of binding constant (K{sub a}) was 10{sup 4}, and the number of binding site (n) in the binary system was approximately equal to 1; electrostatic force played an important role on the conjugation reaction between BSA and CS. On the basis of the Foerster theory of the resonance energy transfer, the binding distance (r) between CS and BSA was less than 7 nm. Comparing the quenching of protein fluorescence excited at 280 nm and 295 nm and from the site marker replacement experiments, it was shown that the primary CS binding site was located in the sub-domain IIA (site I) of BSA. Synchronous fluorescence spectra clearly revealed that the binding of CS with BSA can induce conformation changes in BSA. In addition, the effects of common metal ions on the binding constants of CS-BSA complex were also discussed. It was shown that, except Cu{sup 2+}, the high metal ion concentrations improved the CS efficacy. - Highlights: Black-Right-Pointing-Pointer Complex formation is dominant for the reduction of BSA fluorescence. Black-Right-Pointing-Pointer Primary binding site for drug is located in the sub-domain IIA of BSA. Black-Right-Pointing-Pointer Electrostatic force played a main role between the drug and the BSA. Black-Right-Pointing-Pointer The BSA structure changes upon drug complexation. Black-Right-Pointing-Pointer Higher concentrations of metal ions have good effects to improve efficacy of drug except Cu{sup 2+}.

  8. Electrochemical Immunosensor Based on Polythionine/Gold Nanoparticles for the Determination of Aflatoxin B1

    Directory of Open Access Journals (Sweden)

    Joseph H.O. Owino

    2008-12-01

    Full Text Available An aflatoxin B1 (AFB1 electrochemical immunosensor was developed by the immobilisation of aflatoxin B1-bovine serum albumin (AFB1-BSA conjugate on a polythionine (PTH/gold nanoparticles (AuNP-modified glassy carbon electrode (GCE. The surface of the AFB1-BSA conjugate was covered with horseradish peroxidase (HRP, in order to prevent non-specific binding of the immunosensors with ions in the test solution. The AFB1 immunosensor exhibited a quasi-reversible electrochemistry as indicated by a cyclic voltammetric (CV peak separation (ΔEp value of 62 mV. The experimental procedure for the detection of AFB1 involved the setting up of a competition between free AFB1 and the immobilised AFB1-BSA conjugate for the binding sites of free anti-aflatoxin B1 (anti-AFB1 antibody. The immunosensor’s differential pulse voltammetry (DPV responses (peak currents decreased as the concentration of free AFB1 increased within a dynamic linear range (DLR of 0.6 - 2.4 ng/mL AFB1 and a limit of detection (LOD of 0.07 ng/mL AFB1. This immunosensing procedure eliminates the need for enzyme-labeled secondary antibodies normally used in conventional ELISA–based immunosensors.

  9. Hydrophobic interactions of phenoxazine modulators with bovine serum albumin

    Indian Academy of Sciences (India)

    H N Kalpana; B C Channu; Chhabil Dass; P J Houghton; K N Thimmaiah

    2000-02-01

    The interaction of 10-(3’-N-morpholinopropyl)phenoxazine [MPP], 10-(4’-N-morpholinobutyl)phenoxazine [MBP], 10-(3’-N-morpholinopropyl)-2-chlorophenoxazine [MPCP], 10-(3’-N-piperidinopropyl)-2-chlorophenoxazine [PPCP] or 10-(3’-N-morpholinopropyl)-2-trifluoromethylphenoxazine [MPTP] with bovine serum albumin (BSA) has been studied by gel filtration and equilibrium dialysis methods. The binding of these modulators, based on dialysis experiments, has been characterized using the following parameters: percentage of bound drug (), the association constant (1), the apparent binding constant () and the free energy change ( °). The binding of phenoxazine derivatives to serum transporter protein, BSA, is correlated with their octanol-water partition coefficient, log10 ~ . In addition, effect of the displacing activities of hydroxyzine and acetylsalicylic acid on the binding of phenoxazine derivatives to albumin has been studied. Results of the displacement experiments show that phenoxazine benzene rings and tertiary amines attached to the side chain of the phenoxazine moiety are bound to a hydrophobic area on the albumin molecule.

  10. Binding of several anti-tumor drugs to bovine serum albumin: Fluorescence study

    Energy Technology Data Exchange (ETDEWEB)

    Bi Shuyun [College of Chemistry, Changchun Normal University, Changchun 130032 (China)], E-mail: sy_bi@sina.com; Sun Yantao [College of Chemistry, Jilin University, Changchun 130023 (China); College of Chemistry, Jilin Normal University, Siping 136000 (China); Qiao Chunyu; Zhang Hanqi [College of Chemistry, Jilin University, Changchun 130023 (China); Liu Chunming [College of Chemistry, Changchun Normal University, Changchun 130032 (China)

    2009-05-15

    The interactions of mitomycin C (MMC), fluorouracil (FU), mercaptopurine (MP) and doxorubicin hydrochloride (DXR) with bovine serum albumin (BSA) were studied by spectroscopic method. Quenching of fluorescence of serum albumin by these drugs was found to be a static quenching process. The binding constants (K{sub A}) were 9.66x10{sup 3}, 2.08x10{sup 3}, 8.20x10{sup 2} and 7.50x10{sup 3} L mol{sup -1} for MMC-, FU-, MP- and DXR-BSA, respectively, at pH 7.4 Britton-Robinson buffer at 28 deg. C. The thermodynamic functions such as enthalpy change ({delta}H), entropy change ({delta}S) and Gibbs free-energy change ({delta}G) for the reactions were also calculated according to the thermodynamic equations. The main forces in the interactions of these drugs with BSA were evaluated. It was found that the interactions of MMC and FU with BSA were exothermic processes and those of MP and DXR with BSA were endothermic. In addition, the binding sites on BSA for the four drugs were probed by the changes of binding properties of these drugs with BSA in the presence of two important site markers such as ibuprofen and indomethacin. Based on the Foester theory of non-radiation energy transfer, the binding distances between the drugs and tryptophane were calculated and they were 3.00, 1.14, 2.85, and 2.79 nm for MMC, FU, MP and DXR, respectively.

  11. Investigation on the binding activities of citalopram with human and bovine serum albumins

    Energy Technology Data Exchange (ETDEWEB)

    Lin, Jingjing; Liu, Yan, E-mail: liuyan@fjirsm.ac.cn; Chen, Mingmao; Huang, Huayin; Song, Ling, E-mail: songling@fjirsm.ac.cn

    2014-02-15

    The binding interactions of citalopram (CIT), an efficient antidepressant, with human serum albumin (HSA) and bovine serum albumin (BSA) were investigated by a series of spectroscopic methods including fluorescence, UV–vis absorption, circular dichroism (CD) and {sup 1}H nuclear magnetic resonance ({sup 1}H NMR). The fluorescence quenching and UV–vis absorption studies reveal that CIT could form complexes with both HSA and BSA. The CIT–BSA complex exhibits higher binding affinity than CIT–HSA complex. The thermodynamic study further suggests that the interactions between CIT and SAs are mainly driven by hydrophobic forces and hydrogen bonds. The {sup 1}H NMR analysis indicates that the participation of different functional groups of CIT is unequal in the complexation of CIT–HSA and CIT–BSA. Site marker competitive experiments show that the interactions between CIT and SAs primarily locate at sub-domain II A (site I). The effects of CIT on the conformation of SAs are further analyzed via synchronous fluorescence, three-dimensional fluorescence and CD spectra techniques. The results prove that the presence of CIT decreases the α-helical content of both SAs and induces the slight unfolding of the polypeptides of protein. Additionally, the conformational change of BSA induced by CIT is larger than that of HSA. -- Highlights: • The difference of binding activity between CIT–BSA and CIT–HSA is first reported. • Use spectroscopic, thermodynamic, and NMR methods. • CIT exhibits higher binding affinity to BSA than to HSA. • The binding forces between CIT and SA have been investigated. • The complexation of CIT–SA induces the conformational change of SA.

  12. The interaction between Ag+ and bovine serum albumin: A spectroscopic investigation

    International Nuclear Information System (INIS)

    By using spectroscopic methods, we probed the interaction of Ag+ with bovine serum albumin (BSA) in an aqueous environment. Fluorescence of BSA quenched by Ag+ is a dynamic quenching process. Two binding modes-a strong one at low concentration of Ag+ and a weak one at high concentration were found. The association constant (KA) and the number of binding sites (n) were 4.88 x 103 M-1 and 1.17 for strong binding, and 17.6 M-1 and 0.547 for weak binding at 293 K. The results of thermodynamic parameters ΔHθ, ΔGθ and ΔSθ for instinct binding modes at different temperatures indicated that the hydrogen bonding and van der Waals interaction play a major role for low Ag+/BSA ratio while electrostatic association for high Ag+/BSA ratio. Data of UV-Vis and Circular dichroism (CD) suggested that with the increasing amount of Ag+, the secondary structure undergoes a decrease in α-helix and an increase in β content and the backbone of BSA experiences a micro-environmental alteration. Furthermore, the distance r between donor (Trp-212) and acceptor (Ag+) was evaluated to be 10 nm according to nonradiative energy transfer theory. - Research Highlights: → A spectroscopy-based assessment model was performed to estimate the binding of Ag+ to bovine serum albumin (BSA). → Ag+ was found not only to change the microenvironment of fluorescent amino acid residues of BSA but also to cause alterations in the secondary and tertiary structural content of protein. → Two binding modes occur according to Ag+ concentration, which is different other metal bindings.

  13. Study of Bovine Serum Albumin Solubility in Aqueous Solutions by Intrinsic Viscosity Measurements

    OpenAIRE

    Martin Alberto Masuelli

    2013-01-01

    The behavior of bovine serum albumin (BSA) in water is scarcely studied, and the thermodynamic properties arising from the experimental measurements have not been reported. Intrinsic viscosity measurements are very useful in assessing the interaction between the solute and solvent. This work discussed in a simple determination of the enthalpy of BSA in aqueous solution when the concentration ranges from 0.2 to 36.71% wt. and the temperature from 35 to 40°C. The relationship between the concen...

  14. Physicochemical studies on the interaction of serum albumin with pulmonary surfactant extract in films and bulk bilayer phase.

    Science.gov (United States)

    Nag, Kaushik; Vidyashankar, Sangeetha; Devraj, Ravi; Fritzen Garcia, Mauricia; Panda, Amiya K

    2010-12-15

    Functionality, structure and composition of the adsorbed films of bovine lipid extract surfactant (BLES), in the absence and presence of bovine serum albumin (BSA), at the air-buffer interface was characterized through surface tension, atomic force microscopy and time of flight secondary ion mass spectrometric methods. Gel and fluid domains of BLES films were found to be altered significantly in the presence of BSA. Differential scanning calorimetric studies on BLES dispersions in presence of BSA revealed that the perturbations of the lipid bilayer structures were significant only at higher amount of BSA. FTIR studies on the BLES dispersions in buffer solution revealed that BSA could affect the lipid head-group hydrations in bilayer as well as the methylene and methyl vibration modes of fatty acyl chains of the phospholipids present in BLES. Serum albumin could perturb the film structure at pathophysiological concentration while higher amount of BSA was required in perturbing the bilayer structures. The studies suggest a connected perturbed bilayer to monolayer transition model for surfactant inactivation at the alveolar-air interface in dysfunctional surfactants. PMID:20850129

  15. Influence of galloyl moiety in interaction of epicatechin with bovine serum albumin: a spectroscopic and thermodynamic characterization.

    Directory of Open Access Journals (Sweden)

    Sandip Pal

    Full Text Available The health benefits stemming from green tea are well known, but the exact mechanism of its biological activity is not elucidated. Epicatechin (EC and epicatechin gallate (ECG are two dietary catechins ubiquitously present in green tea. Serum albumins functionally carry these catechins through the circulatory system and eliminate reactive oxygen species (ROS induced injury. In the present study ECG is observed to have higher antioxidant activity; which is attributed to the presence of galloyl moiety. The binding affinity of these catechins to bovine serum albumin (BSA will govern the efficacy of their biological activity. EC and ECG bind with BSA with binding constants 1.0 × 10(6 M(-1 and 6.6 × 10(7 M(-1, respectively. Changes in secondary structure of BSA on interaction with EC and ECG have been identified by circular dichroism (CD and Fourier transform infrared (FT-IR spectroscopy. Thermodynamic characterization reveals the binding process to be exothermic, spontaneous and entropy driven. Mixed binding forces (hydrophobic, electrostatic and hydrogen bonding exist between ECG and BSA. Binding site for EC is primarily site-II in sub-domain IIIA of BSA and for ECG; it is site-I in sub-domain IIA. ECG with its high antioxidant activity accompanied by high affinity for BSA could be a model in drug designing.

  16. Exploring the binding mechanism of ondansetron hydrochloride to serum albumins: Spectroscopic approach

    Science.gov (United States)

    Sandhya, B.; Hegde, Ashwini H.; K. C., Ramesh; Seetharamappa, J.

    2012-02-01

    The mechanism of interaction of ondansetron hydrochloride (OND) to serum albumins [bovine serum albumin (BSA) and human serum albumin (HSA)] was studied for the first time employing fluorimetric, circular dichroism, FTIR and UV-vis absorption techniques under the simulated physiological conditions. Fluorimetric results were utilized to investigate the binding and conformational characteristics of protein upon interaction with varying concentrations of the drug. Higher binding constant values revealed the strong interaction between the drug and protein while the number of binding sites close to unity indicated single class of binding site for OND in protein. Thermodynamic results revealed that both hydrogen bond and hydrophobic interactions played a major role in stabilizing drug-protein complex. Site marker competitive experiments indicated that the OND bound to albumins at subdomin II A (Sudlow's site I). Further, the binding distance between OND and serum albumin was calculated based on the Förster's theory of non-radioactive energy transfer and found to be 2.30 and 3.41 nm, respectively for OND-BSA and OND-HSA. The circular dichroism data revealed that the presence of OND decreased the α-helix content of serum albumins. 3D-fluorescence results also indicated the conformational changes in protein upon interaction with OND. Further, the effects of some cations have been investigated in the interaction of drug to protein.

  17. Exploring the binding mechanism of ondansetron hydrochloride to serum albumins: spectroscopic approach.

    Science.gov (United States)

    B, Sandhya; Hegde, Ashwini H; K C, Ramesh; J, Seetharamappa

    2012-02-01

    The mechanism of interaction of ondansetron hydrochloride (OND) to serum albumins [bovine serum albumin (BSA) and human serum albumin (HSA)] was studied for the first time employing fluorimetric, circular dichroism, FTIR and UV-vis absorption techniques under the simulated physiological conditions. Fluorimetric results were utilized to investigate the binding and conformational characteristics of protein upon interaction with varying concentrations of the drug. Higher binding constant values revealed the strong interaction between the drug and protein while the number of binding sites close to unity indicated single class of binding site for OND in protein. Thermodynamic results revealed that both hydrogen bond and hydrophobic interactions played a major role in stabilizing drug-protein complex. Site marker competitive experiments indicated that the OND bound to albumins at subdomin II A (Sudlow's site I). Further, the binding distance between OND and serum albumin was calculated based on the Förster's theory of non-radioactive energy transfer and found to be 2.30 and 3.41 nm, respectively for OND-BSA and OND-HSA. The circular dichroism data revealed that the presence of OND decreased the α-helix content of serum albumins. 3D-fluorescence results also indicated the conformational changes in protein upon interaction with OND. Further, the effects of some cations have been investigated in the interaction of drug to protein. PMID:22112579

  18. Study of the Interaction of Cephalosporin Class Medicine with Albumin by Fluorescence Enhancement and Fluorescence Quenching Theories

    Institute of Scientific and Technical Information of China (English)

    YANG Man-Man; XI Xiao-Li; YANG Pin

    2006-01-01

    The interaction of 7 kinds of cephalosporin-medicine with HSA and BSA was studied and compared using fluorescence enhancement and fluorescence quenching method, then deeply analyzed. The binding characteristics of medicine with albumin and usual characteristic constants such as dissociation constant, quenching constant,quenching efficiency, energy-transfer efficiency and the distance between donor and accepter were also deeply analyzed.

  19. Studies on Interaction between Gatifloxacin and Bovine Serum Albumin by Spectroscopy

    Institute of Scientific and Technical Information of China (English)

    LIU Xiao-Hui; YE Yan; ZENG Zheng-Zhi

    2007-01-01

    The interaction of gatifloxacin (HGA) with bovine serum albumin (BSA) at 15 and 37 ℃ has been investigated by fluorescence quenching spectroscopy in aqueous solution. The bimolecular quenching rate constant was determined by Stem-Volmer curves and the values were Kq=9.28× 1012 L·mol-1·s-1 (15 ℃) and Kq=8.51 × 1012L·mol-1·s-1 (37 ℃). The results showed that the fluorescence quenching mechanism of BSA by HGA was a static quenching procedure. The thermodynamic parameters indicated that electrostatic forces played major role in the interaction of BSA with HGA. Studies on the relationship between the concentration of HGA and the fluorescence intensity of BSA showed that BSA and HGA bound at the molar ratio 1∶ 1 and the equilibrium constant K0 was 6.80× 104 L·mol 1. The binding distances between BSA and HGA and the energy transfer efficiency were obtained based on the F(o)rster's theory.

  20. Characterization of erythrosine B binding to bovine serum albumin and bilirubin displacement.

    Science.gov (United States)

    Mathavan, Vinodaran M K; Boh, Boon Kim; Tayyab, Saad

    2009-08-01

    The interaction of crythrosine B (ErB), a commonly used dye for coloring foods and drinks, with bovine scrum albumin (BSA) was investigated both in the absence and presence of bilirubin (BR) using absorption and absorption difference spectroscopy. ErB binding to BSA was reflected from a significant red shift of 11 nm in the absorption maximum of ErB (527 nm) with the change in absorbance at lamdamax. Analysis of absorption difference spectroscopic titration results of BSA with increasing concentrations of ErB3 using Benesi-Hildebrand equation gave the association constant, K as 6.9 x 10(4) M(-1). BR displacing action of ErB was revealed by a significant blue shift in the absorption maximum, accompanied by a decrease in absorbance difference at lamdamax in the difference spectrum of BR-BSA complex upon addition of increasing concentrations of ErB. This was further substantiated by fluorescence spectroscopy, as addition of increasing concentrations of ErB to BR-BSA complex caused a significant decrease in fluoresccnce at 510 nm. The results suggest that ErB binds to a site in the vicinity of BR binding site on BSA. Therefore, intake of ErB may increase the risk of hyperbilirubinemia in the healthy subjects. PMID:19788065

  1. The investigation of the interaction between edaravone and bovine serum albumin by spectroscopic approaches

    Energy Technology Data Exchange (ETDEWEB)

    Yu Xianyong; Yang Ying; Liu Ronghua; Huang Haowen; Chen Jian; Ji Danhong [Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201 (China); Li Xiaofang, E-mail: fine_chem@163.co [Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201 (China); Yang Fengxian [Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201 (China); Yi Pinggui, E-mail: pgyi@hnust.c [Key Laboratory of Theoretical Chemistry and Molecular Simulation of Ministry of Education, Hunan Province College Key Laboratory of QSAR/QSPR, School of Chemistry and Chemical Engineering, Hunan University of Science and Technology, Xiangtan 411201 (China)

    2011-07-15

    The fluorescence and ultraviolet spectroscopies were explored to study the interaction between edaravone (EDA) and bovine serum albumin (BSA) under imitated physiological condition. The experimental results show that the fluorescence quenching mechanism between EDA and BSA is a combined quenching (dynamic and static quenching). The binding constants, binding sites, and the corresponding thermodynamic parameters ({Delta}G, {Delta}H, and {Delta}S) of the interaction system were calculated at different temperatures. According to Foerster non-radiation energy transfer theory, the binding distance between EDA and BSA was calculated to be 3.10 nm. The effect of EDA on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. In addition, the effects of some common metal ions Mg{sup 2+}, Ca{sup 2+}, Cu{sup 2+}, and Ni{sup 2+} on the binding constant between EDA and BSA were examined. - Highlights: {yields} We explored the interaction of BSA and EDA using spectroscopic methods. {yields} The fluorescence quenching mechanism is combined quenching. {yields} Hydrophobic interaction force plays a major role in stabilizing the complex. {yields} The binding constants, binding sites, and thermodynamic parameters were calculated. {yields} EDA affects the conformation of tryptophan residue's microregion.

  2. Synthesis of bovine serum albumin imprinted Mn:ZnS quantum dots

    Institute of Scientific and Technical Information of China (English)

    Ming Bo Xu; Tai Ye; Shi Yan Lu; Qin Qin Hu; Juan Zhou; Jian Quan Lu

    2012-01-01

    A novel bovine serum albumin (BSA) imprinted Mn-doped ZnS quantum dots (Mn:ZnS QDs) is firstly reported.The molecular imprinted polymer (MIP) functionalized Mn:ZnS QDs (Mn:ZnS@SiO2@MIP) include the preparation of Mn:ZnS QDs,the coating of silica on the surface of Mn:ZnS QDs,and the functional polymerization by sol-gel reaction using 3-aminophenylboronic acid as the functional and cross-linking monomer in the presence of BSA (Mn:ZnS@SiO2@MIP-BSA),and then the elution of the imprinted BSA on the surface of Mn:ZnS@SiO2 QDs.The results showed that the phosphorescence of Mn:ZnS@SiO2@MIP is stronger quenched by BSA than that of non-imprinted one (Mn:ZnS@SiO2@NIP),indicating that the selectivity of the imprinted Mn:ZnS quantum dots toward BSA is superior to that of non-imprinted one.

  3. Decoration of heparin and bovine serum albumin on polysulfone membrane assisted via polydopamine strategy for hemodialysis.

    Science.gov (United States)

    Xie, Bingwu; Zhang, Ranran; Zhang, Huan; Xu, Anxiu; Deng, Yi; Lv, Yalin; Deng, Feng; Wei, Shicheng

    2016-06-01

    Renal failure brings about abnormality of waste and toxins and deposition in the body. In clinic, the waste and toxins in vitro are eliminated by hemodialysis device with polysulfone (PSF) porous membranes. In the work, decoration of heparin (Hep) and bovine serum albumin (BSA) on PSF membranes would be beneficial to improve the hemocompatibility and reduce the anaphylatoxin formation during hemodialysis. The PSF porous membranes are surface-modified by simply dipping them into dopamine aqueous solution for 8 h. Then, Hep and BSA are immobilized covalently onto the resultant membrane. Attenuated total reflectance Fourier transform infrared spectra (ATR-FTIR) confirms that Hep and BSA are successfully introduced onto the surface of PSF membranes. Scanning electronic microscopy (SEM) and atomic force microscopy (AFM) display the changes of surface morphologies after modification. The result of water contact angle measurement shows that the hydrophilicity of PSF membranes is remarkably improved after coating polydopamine (pDA) and binding Hep and BSA. The experiments of hemocompatibility indicate that Hep and BSA grafted onto membranes suppress the adhesion of platelet and enhance the anticoagulation ability of PSF membranes. Furthermore, the protein adsorption tests reveal that Hep and BSA immobilized onto membranes depress the protein absorption and develop antifouling-protein ability of pristine membrane. This study proves a convenient and simple approach to graft two functional organic polymers which, respectively, play a vital role and then improve the hemocompatibility and biocompatibility of PSF membranes for their biomedical and blood-contacting applications. PMID:27018964

  4. Gold Functionalized Mesoporous Silica Nanoparticle Mediated Protein and DNA Codelivery to Plant Cells Via the Biolistic Method

    Energy Technology Data Exchange (ETDEWEB)

    Martin-Ortigosa, Susana; Valenstein, Justin S.; Lin, Victor S.-Y.; Trewyn, Brian G.; Wang, Kan

    2012-09-11

    The synthesis and characterization of a gold nanoparticle functionalized mesoporous silica nanoparticle (Au-MSN) platform for codelivery of proteins and plasmid DNA to plant tissues using a biolistic particle delivery system is reported. The in vitro uptake and release profiles of fluorescently labeled bovine serum albumin (BSA) and enhanced green fluorescent protein (eGFP) are investigated. As a proof-of-concept demonstration, Au-MSN with large average pore diameters (10 nm) are shown to deliver and subsequently release proteins and plasmid DNA to the same cell after passing through the plant cell wall upon bombardment. Release of fluorescent eGFP indicates the delivery of active, non-denatured proteins to plant cells. This advance represents the first example of biolistic-mediated codelivery of proteins and plasmid DNA to plant cells via gold-functionalized MSN and provides a powerful tool for both fundamental and applied research of plant sciences.

  5. Synthesis and Characterization of Protein-Conjugated Silver Nanoparticles/Silver Salt Loaded Poly (3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV) Film for Prevention of Bacterial Infections and Potential Use in Bone Tissue Engineering Applications

    Science.gov (United States)

    Bakare, Rotimi Ayotunde

    Failure of orthopedic implants due to bacterial infection has been a major concern in bone tissue engineering. To this end, we have formulated a potential orthopedic implant made of naturally occurring biodegradable polymer, i.e. poly (3-hydroxylbutyrate-co-3-hydroxylvalerate) (PHBV), modified with BSA conjugated silver nanoparticles and or silver chloride. Upon release of Ag NPs and or Ag+ in the implant region, can promote aseptic environment by inhibition of bacteria growth and also support/maintain bone cell adhesion, growth, and proliferation. For formulating nanoparticles loaded PHBV scaffold, we exploit specific interaction between bovine serum albumin (BSA) of BSA capped silver nanoparticles and collagen of collagen immobilized PHBV scaffold. Therefore, the first part of this study dealt with synthesis and characterization of collagen immobilized PHBV film for loading of BSA stabilized silver (Ag/BSA) nanoparticles. Two different approaches were used to immobilize collagen on macroporous PHBV film. First approach uses thermal radical copolymerization with 2-hydroxyethylmethacrylate (HEMA), while the second approach uses aminolysis to functionalize macroporous PHBV film. Using collagen crosslinker, type I collagen was covalently grafted to formulate collagen immobilized PHEMA-g-PHBV and collagen immobilized NH2-PHBV films, respectively. Spectroscopic (FTIR, XPS), physical (SEM), and thermal (TGA) techniques were used to characterize the functionalized PHBV films. The Ag/BSA nanoparticles were then loaded on collagen immobilized PHBV films and untreated PHBV films. The concentration of nanoparticles loaded on PHBV film was determined by atomic absorption spectrometry and fluorescence spectroscopy. The amount of nanoparticles loaded on collagen immobilized PHBV film was found to be significantly greater than that on untreated PHBV film. The amount of Ag/BSA nanoparticles loaded on collagen immobilized PHBV film was found to depend on the concentration of Ag/BSA

  6. Gelatin nanoparticles for use as a vaccine adjuvant in intranasal immunizations

    Science.gov (United States)

    Washington, Tara D.

    Vaccine adjuvants are used to increase the immune response in the delivery of subunit antigens. Currently the only FDA approved adjuvants are aluminum based and must be delivered parenterally. Nasal mucoadhesive vaccine administration can decrease cost, increase efficiency and increase patient compliance. The purpose of this study was to develop a mucoadhesive gelatin nanoparticle >500 nm in diameter that can be used to encapsulate a model protein antigen. The particles were prepared by nanoprecipitation of a gelatin solution with acetone. Thiol groups were incubated with gelatin to increase mucoadhesivness at 20, 40, and 80 mg per 1 gram of gelatin. The thiolation chemistry was characterized using UV-Vis and x-ray photoelectron spectroscopy (XPS). The total amount of sulfur present in the gelatin was determined to be 7.48, 30.53, and 46.75 mmol/gram respectively. However XPS analysis revealed that there was no substantial difference between surface sulfur content of the unmodified gelatin nanoparticles and the gelatin nanoparticles modified with 80 mg of iminothiolane. Particle size, charge and morphology were determined using laser light diffraction, atomic force microscopy microscopy and electron microscopy. The average diameter of the unmodified gelatin was 171 nm. The average diameter of the thiolated gelatin nanoparticles was 275 nm. The polydispersity index was approximately 0.61 +/- 0 .04 for all nanoparticles. The zeta (zeta) potential of the unmodified gelatin nanoparticles was -21.5 +/- 2.0 mV and the zeta-potential of the modified gelatin nanoparticles was -25.2 +/- 1.5, -27.3 +/- 0.8, and -28.6 +/- 3.0 mV for the 20, 40, and 80 thiolated gelatin nanoparticles. Particle encapsulation efficiency (EE) and release kinetics were conducted using fluorescein isothiocyanate-bovine serum albumin (FITC-BSA) as a model antigen. The EE of the nanoparticles increased from 35.0% (unmodified gelatin) to 82.5% (highest modified gelatin). Particles encapsulated with

  7. Preparation of bovine serum albumin hollow microparticles by the water-in-oil emulsion solvent diffusion technique for drug delivery applications

    International Nuclear Information System (INIS)

    Biodegradable bovine serum albumin (BSA) hollow microparticles have been prepared by a single step and rapid water-in-oil emulsion solvent diffusion method without any emulsifiers and templates. Aqueous BSA solution and ethyl acetate were used as water and oil phases, respectively. BSA solution was cross-linked with polyethylene glycol diglycidyl ether (PEGDE) before microparticle formation. Methylene blue (MB) was used as a water-soluble model drug to entrap in the microparticle matrix. The non-cross-linked and cross-linked BSA microparticles contained empty core structure with outer smooth surface. Inner surface and matrix of hollow microparticles consisted void structure. Drug loading did not affect the microparticle morphology. Cumulative drug released from microparticles was decreased steadily as decreasing of MB ratio and increasing of PEGDE ratio. The BSA hollow microparticles may have potential application in controlled release drug delivery application. (author)

  8. Antioxidative effects of magnetized extender containing bovine serum albumin on sperm oxidative stress during long-term liquid preservation of boar semen.

    Science.gov (United States)

    Lee, Sang-Hee; Park, Choon-Keun

    2015-08-21

    Magnetized water is defined as water that has passed through a magnet and shows increased permeability into cells and electron-donating characteristics. These attributes can protect against membrane damage and remove reactive oxygen species (ROS) in mammalian cells. We explored the effects of improved magnetized semen extenders containing bovine serum albumin (BSA) as antioxidants on apoptosis in boar sperm. Ejaculated semen was diluted in magnetized extender (0G and 6000G) with or without BSA (0G + BSA and 6000G + BSA), and sperm were analyzed based on viability, acrosome reaction, and H2O2 level of live sperm using flow cytometry. Sperm were then preserved for 11 days at 18 °C. We found that viability was significantly higher in 6000G + BSA than under the other treatments (P boar sperm. PMID:26143531

  9. Interaction of norfloxacin with bovine serum albumin studied by different spectrometric methods; displacement studies, molecular modeling and chemometrics approaches

    Energy Technology Data Exchange (ETDEWEB)

    Naseri, Abdolhossein, E-mail: a_naseri@tabrizu.ac.ir [Departments of Analytical Chemistry, Faculty of Chemistry, University of Tabriz, Tabriz 51666-16471 (Iran, Islamic Republic of); Hosseini, Soheila [Departments of Analytical Chemistry, Faculty of Chemistry, University of Tabriz, Tabriz 51666-16471 (Iran, Islamic Republic of); Rasoulzadeh, Farzaneh [Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of); Rashidi, Mohammad-Reza [Research Center for Pharmaceutical Nanotechnology, Tabriz University of Medical Sciences, Tabriz 51644-14766 (Iran, Islamic Republic of); Zakery, Maryam; Khayamian, Taghi [Department of Chemistry, College of Chemistry, Isfahan University of Technology, Isfahan 84154 (Iran, Islamic Republic of)

    2015-01-15

    Serum albumins as major target proteins can bind to other ligands leading to alteration of their pharmacological properties. The mechanism of interaction between norfloxacin (NFLX) with bovine serum albumin (BSA) was investigated. Fuorescence quenching of serum albumin by this drug was found to be a static quenching process. The binding sites number, n, apparent binding constant, K, and thermodynamic parameters were calculated at different temperatures. The distance, r, between donor, BSA, and acceptor, NFLX, was calculated according to the Forster theory of non-radiation energy transfer. Also binding characteristics of NFLX with BSA together with its displacement from its binding site by kanamycin and effect of common metal ions on binding constant were investigated by the spectroscopic methods. The conformational change in the secondary structure of BSA upon interaction with NFLX was investigated qualitatively from synchronous fluorescence spectra, Fourier Transform Infrared (FTIR) and circular dichroism (CD) spectrometric methods. Molecular docking studies were performed to obtain information on the possible residues involved in the interaction process and changes in accessible surface area of the interacting residues. The results showed that the conformation of BSA changed in the presence of NFLX. For the first time, displacement studies were used for this interaction; displacement studies showed that NFLX was displaced by phenylbutazon and ketoprofen but was not displaced by ibuprofen indicating that the binding site of NFLX on albumin was site I. In addition a powerful chemometrics method, multivariate curve resolution-alternating least square, was used for resolution of spectroscopic augmented data obtained in two different titration modes in order to extract spectral information regardless of spectral overlapping of components. - Highlights: • Interaction between norfloxacin and BSA is studied by spectral methods. • Chemometrics methods are used to

  10. Interaction of norfloxacin with bovine serum albumin studied by different spectrometric methods; displacement studies, molecular modeling and chemometrics approaches

    International Nuclear Information System (INIS)

    Serum albumins as major target proteins can bind to other ligands leading to alteration of their pharmacological properties. The mechanism of interaction between norfloxacin (NFLX) with bovine serum albumin (BSA) was investigated. Fuorescence quenching of serum albumin by this drug was found to be a static quenching process. The binding sites number, n, apparent binding constant, K, and thermodynamic parameters were calculated at different temperatures. The distance, r, between donor, BSA, and acceptor, NFLX, was calculated according to the Forster theory of non-radiation energy transfer. Also binding characteristics of NFLX with BSA together with its displacement from its binding site by kanamycin and effect of common metal ions on binding constant were investigated by the spectroscopic methods. The conformational change in the secondary structure of BSA upon interaction with NFLX was investigated qualitatively from synchronous fluorescence spectra, Fourier Transform Infrared (FTIR) and circular dichroism (CD) spectrometric methods. Molecular docking studies were performed to obtain information on the possible residues involved in the interaction process and changes in accessible surface area of the interacting residues. The results showed that the conformation of BSA changed in the presence of NFLX. For the first time, displacement studies were used for this interaction; displacement studies showed that NFLX was displaced by phenylbutazon and ketoprofen but was not displaced by ibuprofen indicating that the binding site of NFLX on albumin was site I. In addition a powerful chemometrics method, multivariate curve resolution-alternating least square, was used for resolution of spectroscopic augmented data obtained in two different titration modes in order to extract spectral information regardless of spectral overlapping of components. - Highlights: • Interaction between norfloxacin and BSA is studied by spectral methods. • Chemometrics methods are used to

  11. Interaction of bovine serum albumin with a psychotropic drug alprazolam: Physicochemical, photophysical and molecular docking studies

    International Nuclear Information System (INIS)

    The interaction between alprazolam (Alp) and bovine serum albumin (BSA) has been investigated under physiological conditions by UV–vis, steady state as well as time-resolved fluorescence, circular dichroism (CD) spectroscopic and molecular docking studies. The binding constant K of Alp to BSA was found to be 1.8×105 L mol−1 from absorption data. Fluorometric studies suggested the formation of the Alp–BSA complex, while time-resolved fluorescence studies showed that the binding of Alp by BSA was mainly static and the effective rate constant is found to be 2.33×1013 L mol−1 s−1. According to the modified Stern–Volmer equation, the Stern–Volmer quenching constants (KSV) between Alp and BSA at four different temperatures 295, 303, 308, 313 K were obtained to be 1.19×105, 1.05×105, 0.99×105 and 0.90×105 L mol−1, respectively. The change in enthalpy (ΔH) and entropy (ΔS) were calculated to be −11.66 and 57.64 J mol−1 K−1, respectively, indicating that the interaction was hydrophobic in nature. Site marker competitive experiments suggested that the binding of Alp to BSA primarily took place in sub-domain IIA, whereas the binding distance (r) between Alp and the tryptophan residue of BSA was obtained to be 1.87 nm by Förster's theory of non-radiative energy transfer. The conformational studies by CD spectroscopy showed that the presence of Alp decreased the α-helical content of BSA and induced the unfolding of the polypeptide of the protein. The change in conformation was also supported by excitation–emission matrix spectroscopy (EEMS) studies. The molecular docking experiment supports the above results and effectively proves the binding of Alp to BSA. -- Highlights: • Alprazolam: a benzodiazepine drug with anxiolytic and anticonvulsant properties. • Alprazolam induces conformational change on the native as well as urea denatured BSA. • Alprazolam may interfere with serum albumin function in the long run

  12. Interaction of bovine serum albumin with a psychotropic drug alprazolam: Physicochemical, photophysical and molecular docking studies

    Energy Technology Data Exchange (ETDEWEB)

    Sarkar, Moumita; Paul, Shiv Shankar; Mukherjea, Kalyan K., E-mail: k_mukherjea@yahoo.com

    2013-10-15

    The interaction between alprazolam (Alp) and bovine serum albumin (BSA) has been investigated under physiological conditions by UV–vis, steady state as well as time-resolved fluorescence, circular dichroism (CD) spectroscopic and molecular docking studies. The binding constant K of Alp to BSA was found to be 1.8×10{sup 5} L mol{sup −1} from absorption data. Fluorometric studies suggested the formation of the Alp–BSA complex, while time-resolved fluorescence studies showed that the binding of Alp by BSA was mainly static and the effective rate constant is found to be 2.33×10{sup 13} L mol{sup −1} s{sup −1}. According to the modified Stern–Volmer equation, the Stern–Volmer quenching constants (K{sub SV}) between Alp and BSA at four different temperatures 295, 303, 308, 313 K were obtained to be 1.19×10{sup 5}, 1.05×10{sup 5}, 0.99×10{sup 5} and 0.90×10{sup 5} L mol{sup −1}, respectively. The change in enthalpy (ΔH) and entropy (ΔS) were calculated to be −11.66 and 57.64 J mol{sup −1} K{sup −1}, respectively, indicating that the interaction was hydrophobic in nature. Site marker competitive experiments suggested that the binding of Alp to BSA primarily took place in sub-domain IIA, whereas the binding distance (r) between Alp and the tryptophan residue of BSA was obtained to be 1.87 nm by Förster's theory of non-radiative energy transfer. The conformational studies by CD spectroscopy showed that the presence of Alp decreased the α-helical content of BSA and induced the unfolding of the polypeptide of the protein. The change in conformation was also supported by excitation–emission matrix spectroscopy (EEMS) studies. The molecular docking experiment supports the above results and effectively proves the binding of Alp to BSA. -- Highlights: • Alprazolam: a benzodiazepine drug with anxiolytic and anticonvulsant properties. • Alprazolam induces conformational change on the native as well as urea denatured BSA. • Alprazolam may

  13. Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study

    Energy Technology Data Exchange (ETDEWEB)

    Pacheco, Maria E. [Division Quimica Analitica, Departamento de Quimica, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, La Plata, Buenos Aires (Argentina); Bruzzone, Liliana, E-mail: bruzzone@quimica.unlp.edu.ar [Division Quimica Analitica, Departamento de Quimica, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, La Plata, Buenos Aires (Argentina)

    2012-10-15

    The interaction between imazethapyr (IMA) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy. The Stern-Volmer quenching constant (K{sub SV}) at three temperatures was evaluated in order to determine the quenching mechanism. The dependence of fluorescence quenching on viscosity was also evaluated for this purpose. The results showed that IMA quenches the fluorescence intensity of BSA through a static quenching process. The values of the binding constant for the formed BSA-IMA complex and the number of binding sites were found to be 1.51 Multiplication-Sign 10{sup 5} M{sup -1} and 0.77, respectively, at room temperature. Based on the calculated thermodynamic parameters, the forces that dominate the binding process are hydrogen bonds and van der Waals forces, and the binding process is spontaneous and exothermic. The quenching of protein fluorescence by iodide ion was used to probe the accessibility of tryptophan residues in BSA and the change in accessibility induced by the presence of IMA. According to the obtained results, the BSA-IMA complex is formed in the site where the Trp-134 is located, causing it to become less exposed to the solvent. - Highlights: Black-Right-Pointing-Pointer Fluorescence spectroscopy helps to understand protein binding mechanisms. Black-Right-Pointing-Pointer Quenching measurements reveal the nature of the binding process involved. Black-Right-Pointing-Pointer Iodine ion can be used to study the change in accessibility of tryptophan residues. Black-Right-Pointing-Pointer Thermodynamic parameters for the binding reaction confirm binding modes.

  14. Neurochemical sensitization associated with systemic administration of tumor necrosis factor-alpha: adjuvant action in combination with bovine serum albumin.

    Science.gov (United States)

    Anisman, Hymie; Turrin, Nicolas P; Merali, Zul; Hayley, Shawn

    2003-12-01

    Tumor necrosis factor-alpha (TNF-alpha) provokes a time-dependent sensitization of brain monoamine activity, plasma corticosterone activity and sickness behavior, the latter being reminiscent of septic or anaphylactic shock. In this investigation, bovine serum albumin (BSA) elicited similar corticosterone and sickness profiles, whereas the monoamine changes were not observed. The sensitization elicited by mTNF-alpha plus BSA was markedly greater than that elicited by BSA alone. Carrier-free TNF-alpha promoted the sensitization of brain monoamine activity, but not sickness or corticosterone. It is suggested that mTNF-alpha acts as an adjuvant to the anaphylactic actions elicited by BSA, but may provoke a sensitization of monoamine activity which is time-dependent and varies across brain regions. PMID:14644035

  15. Effect of ionic micellar medium on kinetics and mechanism of oxidation of bovine serum albumin: A pulse radiolysis study

    International Nuclear Information System (INIS)

    Effect of protein-micelle interaction on bovine serum albumin (BSA) oxidation by trichloromethyl peroxyl radical (CCl3O2.) in anionic sodium dodecyl sulfate (SDS) and cationic cetyltrimethyl ammonium bromide (CTAB) micellar media has been studied using nanosecond pulse radiolysis technique. Viscosity measurement and light scattering studies have suggested that SDS and CTAB micelles produce BSA-micelle aggregates of different sizes and polydispersity. Oxidation kinetics and transients have been affected both by anionic SDS and cationic CTAB micelles but in a different manner. Tryptophanyl-CCl3O2. adduct radical to tyrosyl radical transformation in BSA has been observed in anionic SDS micelles but not in cationic CTAB micelles. Similar studies have also been done with tryptophan and tyrosine amino acids, which undergo oxidation in BSA. The study suggests that Coulombic and hydrophobic interactions between micelles and protein affect the structure of the protein to shield its functional amino acids, like tryptophan and tyrosine, to neutral oxidizing radical.

  16. RGD偶联吉西他滨白蛋白纳米粒对胰腺癌细胞增殖抑制作用的研究%Study on inhibitory effects of RGD-conjugated gemcitabine-loaded albumin nanoparticles on the proliferation of BxPC-3 cells in vitro

    Institute of Scientific and Technical Information of China (English)

    吉顺荣; 吴闻哲; 王浩; 张波; 刘辰; 龙江; 虞先濬; 倪泉兴; 徐近

    2011-01-01

    Objective To explore the inhibitory effects of RGD-conjugated gemcitabine (GEM)-loaded albumin nanoparticles (ANP) on the proliferation of BxPC-3 cells in vitro. Methods Human pancreatic carcinoma BxPC-3 cells were cultured and then treated 5 different combinations of drugs (BSANP controls, RGD-BSANP, BSANP-GEM, GEM and RGD-BSANP-GEM) respectively. The inhibition rate of BxPC-3 cells was detected by MTT. Results The gemcitabine-loaded albumin nanoparticles produced higher inhibitory effects than gemcitabine alone. The RGD-conjugated gemcitabine-loaded albumin nanoparticles produced even higher anti-proliferation rate than those without RGD conjugation. Conclusions RGD peptides can increase the anti-proliferation rate of gemcitabine-loaded albumin nanoparticles on BxPC-3 cells in vitro.%目的:通过体外试验,探讨RGD偶联吉西他滨白蛋白纳米粒(RGD-BSANP-GEM)对胰腺癌细胞株BxPC-3的体外增殖的抑制作用.方法:以人胰腺癌细胞株BxPC-3为研究对象,分为5个给药组:BSANP对照组、RGD-BSANP组、BSANP-GEM组、GEM原药组、RGD-BSANP-GEM组.运用MTT法检测给药后24h、48 h和72 h的增殖抑制率.结果:BSANP-GEM组细胞抑制率高于GEM组(P<0.05),RGD-BSANP-GEM组细胞抑制率高于BSANP-GEM组.同时RGD-BSANP-GEM组对胰腺癌细胞株的抑制率与给药浓度和作用时间呈正相关.结论:体外RGD环肽能够增加BSANP-GEM对胰腺癌细胞的增殖抑制作用.

  17. Interactions of aptamers with sera albumins

    Science.gov (United States)

    Cortez, Célia Martins; Silva, Dilson; Silva, Camila M. C.; Missailidis, Sotiris

    2012-09-01

    The interactions of two short aptamers to human and bovine serum albumins were studied by fluorescence spectroscopic techniques. Intrinsic fluorescence of BSA and HSA were measured by selectively exciting their tryptophan residues. Gradual quenching was observed by titration of both proteins with aptamers. Aptamers are oligonucleic acid or peptide molecules that bind a specific target and can be used for both biotechnological and clinical purposes, since they present molecular recognition properties like that commonly found in antibodies. Two aptamers previously selected against the MUC1 tumour marker were used in this study, one selected for the protein core and one for the glycosylated MUC1. Stern-Volmer graphs were plotted and quenching constants were estimated. Plots obtained from experiments carried out at 25 °C and 37 °C showed the quenching of fluorescence of by aptamers to be a collisional phenomenon. Stern-Volmer constants estimated for HSA quenched by aptamer A were 1.68 × 105 (±5 × 103) M-1 at 37 °C, and 1.37 × 105 (±103) M-1 at 25 °C; and quenched by aptamer B were 1.67 × 105 (±5 × 103) M-1 at 37 °C, and 1.32 × 105 (±103) M-1 at 25 °C. Results suggest that the primary binding site for aptamers on albumin is close to tryptophan residues in sub domain IIA.

  18. Study on Interaction of Ginsenosides with Bovine or Human Serum Albumin Using Wavelength Modulation Surface Plasmon Resonance Biosensor

    Institute of Scientific and Technical Information of China (English)

    LIU Xia; SUN Ying; SONG Da-Qian; LI Xu-Wen; ZHANG Qing-Lin; TIAN Yuan; LIU Zhong-Ying; ZHANG Han-Qi

    2006-01-01

    To use a newly developed wavelength modulation surface plasmon resonance (SPR) biosensor, an experimental protocol was developed to investigate the interaction of ginsenosides with serum albumin. With a known concentration of the ginsenosides, bound percentages of the ginsenosides with human serum albumin (HSA) or bovine serum albumin (BSA) were obtained. SPR technique could require no labeling and this method provided the detailed information on association and disassociation of molecules in real time. The results indicate that the sensitivity of wavelength modulation SPR biosensor is sufficient for detection and characterization of binding events involving low-molecular weight compounds and their immobilized protein targets.

  19. Effects of caffeic acid and bovine serum albumin in reducing the rate of development of rancidity in oil-in-water and water-in-oil emulsions

    OpenAIRE

    Conde, Enma; Gordon, Micheal H.; Moure, Andres; Dominguez, Herminia

    2011-01-01

    The antioxidant properties of caffeic acid and bovine serum albumin in oil-in-water and water-in-oil emulsions were studied. Caffeic acid (5 mmol/kg emulsion) showed good antioxidant properties in both 30% sunflower oil-in-water (OW) and 20% water-in-sunflower oil emulsions (WO), pH 5.4, during storage at 50 ºC. Although bovine serum albumin (BSA) (0.2%) had a slight antioxidant effect, the combination of caffeic acid and BSA showed a synergistic reduction in the rate of development of rancid...

  20. Study on the interaction between amphiphilic drug and bovine serum albumin: A thermodynamic and spectroscopic description

    International Nuclear Information System (INIS)

    Herein we report the interaction of amphiphilic drug clomipramine hydrochloride (CLP—a tricyclic antidepressant) with bovine serum albumin (BSA) studied by fluorescence, UV–vis, and circular dichroism (CD) spectroscopic techniques. Clomipramine hydrochloride is used to treat a variety of mental health problems. The quenching rate constant (kq) values, calculated according to the fluorescence data, decrease with increase in temperature indicating the static quenching procedure for the CLP–BSA interaction. The association binding constants (KA), evaluated at different conditions, and the thermodynamic parameters (free energy, enthalpy and entropy changes) indicate that the hydrophobic forces play a major role in the binding interaction of drug. The interaction of BSA with CLP was further confirmed by UV absorption spectra. Blue shift of position was detected due to the complex formation between the BSA–CLP. The molecular distance, r0, between donor (BSA) and acceptor (CLP) was estimated by fluorescence resonance energy transfer (FRET) whose value (4.47 nm) suggests high probability of static quenching interaction. The CD results prove the conformational changes in the BSA on binding with the drug. Thus, the results supply qualitative and quantitative understanding of the binding of BSA to CLP, which is important in understanding their effect as therapeutic agents. - Highlights: • BSA can be considered as a good carrier for transportation of CLP in vivo. • The fluorescence results indicated the presence of static quenching mechanism in the binding process. • CD spectra showed the change in molecular conformation of BSA in the presence of CLP. • The results have applicability in model drug delivery

  1. Study on the interaction between amphiphilic drug and bovine serum albumin: A thermodynamic and spectroscopic description

    Energy Technology Data Exchange (ETDEWEB)

    Rub, Malik Abdul, E-mail: malikrub@gmail.com [Chemistry Department, Faculty of Science, King Abdulaziz University, Jeddah-21589 (Saudi Arabia); Khan, Javed Masood [Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002 (India); Asiri, Abdullah M. [Chemistry Department, Faculty of Science, King Abdulaziz University, Jeddah-21589 (Saudi Arabia); Center of Excellence for Advanced Materials Research, King Abdulaziz University, Jeddah-21589 (Saudi Arabia); Khan, Rizwan Hasan, E-mail: rizwanhkhan1@gmail.com [Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002 (India); Kabir-ud-Din [Department of Applied Chemistry, Aligarh Muslim University, Aligarh-202002 (India)

    2014-11-15

    Herein we report the interaction of amphiphilic drug clomipramine hydrochloride (CLP—a tricyclic antidepressant) with bovine serum albumin (BSA) studied by fluorescence, UV–vis, and circular dichroism (CD) spectroscopic techniques. Clomipramine hydrochloride is used to treat a variety of mental health problems. The quenching rate constant (k{sub q}) values, calculated according to the fluorescence data, decrease with increase in temperature indicating the static quenching procedure for the CLP–BSA interaction. The association binding constants (K{sub A}), evaluated at different conditions, and the thermodynamic parameters (free energy, enthalpy and entropy changes) indicate that the hydrophobic forces play a major role in the binding interaction of drug. The interaction of BSA with CLP was further confirmed by UV absorption spectra. Blue shift of position was detected due to the complex formation between the BSA–CLP. The molecular distance, r{sub 0}, between donor (BSA) and acceptor (CLP) was estimated by fluorescence resonance energy transfer (FRET) whose value (4.47 nm) suggests high probability of static quenching interaction. The CD results prove the conformational changes in the BSA on binding with the drug. Thus, the results supply qualitative and quantitative understanding of the binding of BSA to CLP, which is important in understanding their effect as therapeutic agents. - Highlights: • BSA can be considered as a good carrier for transportation of CLP in vivo. • The fluorescence results indicated the presence of static quenching mechanism in the binding process. • CD spectra showed the change in molecular conformation of BSA in the presence of CLP. • The results have applicability in model drug delivery.

  2. Spectroscopic investigation on the interaction of maslinic acid with bovine serum albumin

    Energy Technology Data Exchange (ETDEWEB)

    Molina-Bolívar, J.A., E-mail: jmb@uma.es [Department of Applied Physics II, Engineering School, University of Málaga, 29071 Málaga (Spain); Galisteo-González, F. [Department of Applied Physics, University of Granada, 18071 Granada (Spain); Carnero Ruiz, C. [Department of Applied Physics II, Engineering School, University of Málaga, 29071 Málaga (Spain); Medina-O' Donnell, M.; Parra, A. [Department of Organic Chemistry, University of Granada, 18071 Granada (Spain)

    2014-12-15

    Ultraviolet–visible (UV–vis), steady-state and time-resolved fluorescence, and Fourier transform-infrared (FT-IR) spectroscopy were used to study the interaction between maslinic acid (MA) and bovine serum albumin (BSA). Binding constants were determined at three different temperatures (298, 304, and 310 K). Spectroscopic analysis revealed that the fluorescence-quenching mechanism between MA and BSA was a static quenching procedure. MA specifically binds to one site of the BSA molecule forming a stable complex with a binding constant of (5.4±0.4)×10{sup 4} M{sup −1} at pH 7.4 and 298 K. From the thermodynamic parameters of the binding process (ΔG{sup 0}, ΔH{sup 0} and ΔS{sup 0}) it can be inferred that hydrogen bonds and van der Waals interactions are the predominant intermolecular forces responsible for the stabilization of the complex. Anisotropy studies revealed that tryptophan residues of BSA undergo motion restrictions as a result of the interaction with MA. The distance between MA and the fluorophore residue of BSA was evaluated according to the theory of Föster for fluorescence resonance energy transfer (FRET). Observations from FT-IR spectra and three-dimensional fluorescence indicated changes in the conformation of BSA upon ligand binding. - Highlights: • The interaction between MA and BSA was examined with spectroscopic techniques. • The interaction between MA and BSA was studied at different temperatures. • Fluorescence spectroscopy studies suggest that quenching mechanism is static. • The hydrogen bonds and van der Waals interactions are predominant forces. • Conformational changes of the protein upon binding of MA were observed.

  3. Highly sensitive detection of bovine serum albumin based on the aggregation of triangular silver nanoplates

    Science.gov (United States)

    Zhang, Ling Ling; Ma, Fang Fang; Kuang, Yang Fang; Cheng, Shu; Long, Yun Fei; Xiao, Qiu Guo

    2016-02-01

    A simple, fast and highly sensitive spectrophotometric method for the determination of bovine serum albumin (BSA) has been developed based on the interactions between triangular silver nanoplates (TAgNPs) and BSA in the presence of Britton-Robison buffer solution (BR). Particularly, the wavelength of absorption maximum (λmax) of TAgNPs is red shifted in the presence of BSA together with Britton-Robinson buffer solution (BR, pH = 2.56), and the color of the solution changed from blue to light blue. This may be due to the interactions between BSA molecules on the surface of TAgNPs through electrostatic forces, hydrogen bonds, hydrophobic effects and van der Waals forces at pH 2.56, which leads to the aggregation of TAgNPs. The determination of BSA was achieved by measuring the change of λmax corresponding to localized surface plasmon resonance (LSPR) from UV-visible spectrophotometry. It was found that the shift value in the wavelength of absorption maximum (Δλ, the difference in absorption maxima of the TAgNPs/BSA/BR mixture and the TAgNPs/BR mixture) was proportionate to the concentration of BSA in the range of 1.0 ng mL- 1 to 100.0 ng mL- 1 with the correlation coefficient of r = 0.9969. The detection limit (3 σ/k) for BSA was found to be as low as 0.5 ng mL- 1.

  4. Blood serum and BSA, but neither red blood cells nor hemoglobin can support vitellogenesis and egg production in the dengue vector Aedes aegypti

    Directory of Open Access Journals (Sweden)

    Kristina K. Gonzales

    2015-05-01

    Full Text Available Aedes aegypti is the major vector of dengue, yellow fever and chikungunya viruses that put millions of people in endemic countries at risk. Mass rearing of this mosquito is crucial for strategies that use modified insects to reduce vector populations and transmission of pathogens, such as sterile insect technique or population replacement. A major problem for vector mosquito mass rearing is the requirement of vertebrate blood for egg production since it poses significant costs as well as potential health hazards. Also, regulations for human and animal use as blood source can pose a significant obstacle. A completely artificial diet that supports egg production in vector mosquitoes can solve this problem. In this study, we compared different blood fractions, serum and red blood cells, as dietary protein sources for mosquito egg production. We also tested artificial diets made from commercially available blood proteins (bovine serum albumin (BSA and hemoglobin. We found that Ae. aegypti performed vitellogenesis and produced eggs when given whole bovine blood, serum, or an artificial diet containing BSA. Conversely, egg production was impaired after feeding of the red blood cell fraction or an artificial diet containing only hemoglobin. We also found that egg viability of serum-fed mosquitoes were comparable to that of whole blood and an iron supplemented BSA meal produced more viable eggs than a meal containing BSA alone. Our results indicate that serum proteins, not hemoglobin, may replace vertebrate blood in artificial diets for mass mosquito rearing.

  5. Blood serum and BSA, but neither red blood cells nor hemoglobin can support vitellogenesis and egg production in the dengue vector Aedes aegypti.

    Science.gov (United States)

    Gonzales, Kristina K; Tsujimoto, Hitoshi; Hansen, Immo A

    2015-01-01

    Aedes aegypti is the major vector of dengue, yellow fever and chikungunya viruses that put millions of people in endemic countries at risk. Mass rearing of this mosquito is crucial for strategies that use modified insects to reduce vector populations and transmission of pathogens, such as sterile insect technique or population replacement. A major problem for vector mosquito mass rearing is the requirement of vertebrate blood for egg production since it poses significant costs as well as potential health hazards. Also, regulations for human and animal use as blood source can pose a significant obstacle. A completely artificial diet that supports egg production in vector mosquitoes can solve this problem. In this study, we compared different blood fractions, serum and red blood cells, as dietary protein sources for mosquito egg production. We also tested artificial diets made from commercially available blood proteins (bovine serum albumin (BSA) and hemoglobin). We found that Ae. aegypti performed vitellogenesis and produced eggs when given whole bovine blood, serum, or an artificial diet containing BSA. Conversely, egg production was impaired after feeding of the red blood cell fraction or an artificial diet containing only hemoglobin. We also found that egg viability of serum-fed mosquitoes were comparable to that of whole blood and an iron supplemented BSA meal produced more viable eggs than a meal containing BSA alone. Our results indicate that serum proteins, not hemoglobin, may replace vertebrate blood in artificial diets for mass mosquito rearing. PMID:26020000

  6. Synthesis of an oxytetracyline-tolidin-BSA immunogen and antibodies production of anti-oxytetracyline developed for oxytetracyline residue detection with enzyme-linked immunosorbent assays technique

    Directory of Open Access Journals (Sweden)

    Widiastuti R

    2013-06-01

    Full Text Available An oxytetracycline-tolidin-bovine serum albumin (OTC-tolidin-BSA-conjugate was synthezed as immunogen for producing specific antibodies in immunized rabbits that would be used as reagent for development of OTC residue detection with enzym-linked immunoassays technique. The immunogen was prepared through diazotization tolidin and subsequently reacted with OTC. The red purple immunogen of OTC-tolidin-BSA absorbed at wave lengths of 277 nm and 488 nm under UV screening absorbances and confirmation with the high performance liquid chromatography (HPLC showed the absence of peak at retention time of 3.46 minutes. Characaterized result with SDS-PAGE showed the molecular weight of the OTC-tolidin-BSA at 69.79 kDA. Subsequently, the immunogen was immunized into New Zealand rabbits in order to produce the polyclonal antibodies. The antibodies were purified using a protein A sepharose column. The OD optimum responses of 0.92 to 1.20 were obtained from the second fractionation at dilution of 1/1000 by titrating the antibodies and OTC-tolidin-BSA coating antigen at concentration of 10 µg/mL on several bleeding times.

  7. Selective binding of proteins on functional nanoparticles via reverse charge parity model: an in vitro study

    Science.gov (United States)

    Ghosh, Goutam; Panicker, Lata; Barick, K. C.

    2014-03-01

    The conformation of proteins absorbed on nanoparticles surface plays a crucial role in applications of nanoparticles in biomedicine. The surface protein conformation depends on several factors, namely, nature of protein-nanoparticles interaction, chemical composition of the surface of nanoparticles etc. A model of the electrostatic binding of proteins on charged surface nanoparticles has been proposed earlier (Ghosh et al 2013 Colloids Surf. B 103 267). Also, the irreversible denaturation of the protein conformation due to binding of counterions was reported. In this paper, we have used this model, involving reverse charge parity, to show selective binding of proteins on charged surface iron oxide nanoparticles (IONPs). IONPs were surface functionalized with cetylpyridinium chloride (CPC), cetyl(trimethyl)ammonium bromide (CTAB) and cetylpyridinium iodide (CPI). The effect of counterions (Cl-, Br- and I-) on protein conformation has also been investigated. Several proteins such as α-lactalbumin (ALA), β-lactoglobulin (BLG), ovalbumin (OVA), bovin serum albumin (BSA) and HEWL were chosen for this investigation.

  8. Selective binding of proteins on functional nanoparticles via reverse charge parity model: an in vitro study

    International Nuclear Information System (INIS)

    The conformation of proteins absorbed on nanoparticles surface plays a crucial role in applications of nanoparticles in biomedicine. The surface protein conformation depends on several factors, namely, nature of protein-nanoparticles interaction, chemical composition of the surface of nanoparticles etc. A model of the electrostatic binding of proteins on charged surface nanoparticles has been proposed earlier (Ghosh et al 2013 Colloids Surf. B 103 267). Also, the irreversible denaturation of the protein conformation due to binding of counterions was reported. In this paper, we have used this model, involving reverse charge parity, to show selective binding of proteins on charged surface iron oxide nanoparticles (IONPs). IONPs were surface functionalized with cetylpyridinium chloride (CPC), cetyl(trimethyl)ammonium bromide (CTAB) and cetylpyridinium iodide (CPI). The effect of counterions (Cl−, Br− and I−) on protein conformation has also been investigated. Several proteins such as α-lactalbumin (ALA), β-lactoglobulin (BLG), ovalbumin (OVA), bovin serum albumin (BSA) and HEWL were chosen for this investigation. (papers)

  9. Nanogels fabricated from bovine serum albumin and chitosan via self-assembly for delivery of anticancer drug.

    Science.gov (United States)

    Wang, Yuntao; Xu, Shasha; Xiong, Wenfei; Pei, Yaqiong; Li, Bin; Chen, Yijie

    2016-10-01

    In this study, bovine serum albumin (BSA) and chitosan (CS) were used to prepare BSA-CS nanogels by a simple green self-assembly technique. Then the nanogels were successfully used to entrap doxorubicin hydrochloride (DOX) with an entrapment ratio of 46.3%, aiming to realize the slow-release effect and lower the cytotoxicity of DOX. The IC50 values of DOX-loaded BSA-CS (DOX-BSA-CS) and free DOX obtained by MTT assay in SGC7901 cells were 0.22 and 0.05μg/mL, respectively. The cytotoxicity of DOX significantly decreased within 24h after encapsulation by the nanogels, indicating that the loaded drug could slowly release within 24h and the BSA-CS was a good slow release system. The cellular uptake experiments indicated DOX-BSA-CS diffused faster into the cancer cell than the bare drug. The flow cytometry and TUNEL assay proved DOX-BSA-CS could induce a larger apoptosis proportion of gastric cancer cells 7901 than the bare drug and it is promising to be used for curing gastric cancer. PMID:27262260

  10. [Intermolecular Interactions between Cytisine and Bovine Serum Albumin A Synchronous Fluorescence Spectroscopic Analysis and Molecular Docking Research].

    Science.gov (United States)

    Wu, Yu-hang; Han, Zhong-bao; Ma, Jia-ze; He, Yan; Liu, Li-yan; Xin, Shi-gang; Yu, Zhan

    2016-03-01

    Cytisine (Cy) is one of the alkaloids that exist naturally in the plant genera Laburnum of the family Fabaceae. With strong bioactivities, Cy is commercialized for smoking cessation for years. In this work, the study of intermolecular interactions between Cy and bovine serum albumin (BSA) was performed by applying fluorescence spectroscopic methods under simulated physiological conditions. The mechanism of fluorescence quenching of BSA by Cy was also studied. Parameters such as bathing temperature, time and solution pH were investigated to optimize the fluorescence quenching. The binding type, binding ratio and binding constant between BSA and Cy were calculated by using the Stem-Volmer equation. Experimental results indicated that Cy can quench the fluorescent emission of BSA statically by forming a 1 : 1 type non-covalent complex and the binding constant is 5.6 x 10(3) L x mol(-1). Synchronous fluorescence spectral research shows Cy may affect the fluorescence emission of Trp residues of BSA. Furthermore, molecular docking is utilized to model the complex and probe the plausible quenching mechanism. It can be noted that the hydrogen bindings and hydrophobic interactions between Cy and BSA change the micro-environment of Trp213, which leads to the fluorescence quenching of BSA. PMID:27400521

  11. Role of pH-induced structural change in protein aggregation in foam fractionation of bovine serum albumin

    Directory of Open Access Journals (Sweden)

    Rui Li

    2016-03-01

    Full Text Available For reducing protein aggregation in foam fractionation, the role of pH-induced structural change in the interface-induced protein aggregation was analyzed using bovine serum albumin (BSA as a model protein. The results show that the decrease in pH from 7.0 to 3.0 gradually unfolded the BSA structure to increase the molecular size and the relative content of β-sheet and thus reduced the stability of BSA in the aqueous solution. At the isoelectric point (pH 4.7, BSA suffered the lowest level in protein aggregation induced by the gas–liquid interface. In the pH range from 7.0 to 4.7, most BSA aggregates were formed in the defoaming process while in the pH range from 4.7 to 3.0, the BSA aggregates were formed at the gas–liquid interface due to the unfolded BSA structure and they further aggregated to form insoluble ones in the desorption process.

  12. Serum albumin forms a lactoferrin-like soluble iron-binding complex in presence of hydrogen carbonate ions.

    Science.gov (United States)

    Ueno, Hiroshi M; Urazono, Hiroshi; Kobayashi, Toshiya

    2014-02-15

    The iron-lactoferrin complex is a common food ingredient because of its iron-solubilizing capability in the presence of hydrogen carbonate ions. However, it is unclear whether the formation of a stable iron-binding complex is limited to lactoferrin. In this study, we investigated the effects of bovine serum albumin (BSA) on iron solubility and iron-catalyzed lipid oxidation in the presence of hydrogen carbonate ions. BSA could solubilize >100-fold molar equivalents of iron at neutral pH, exceeding the specific metal-binding property of BSA. This iron-solubilizing capability of BSA was impaired by thermally denaturing BSA at ≥ 70 °C for 10 min at pH 8.5. The resulting iron-BSA complex inhibited iron-catalyzed oxidation of soybean oil in a water-in-oil emulsion measured using the Rancimat test. Our study is the first to show that BSA, like lactoferrin, forms a soluble iron-binding complex in the presence of hydrogen carbonate ions. PMID:24128453

  13. Modulation of the antioxidant activity of HO* scavengers by albumin binding: a 19F-NMR study.

    Science.gov (United States)

    Aime, Silvio; Digilio, Giuseppe; Bruno, Erik; Mainero, Valentina; Baroni, Simona; Fasano, Mauro

    2003-08-01

    The interaction between different HO(z.rad;) radical scavengers in a three-component antioxidant system has been investigated by means of 19F-NMR spectroscopy. This system is composed of bovine serum albumin (BSA), trolox, and N-(4-hydroxyphenyl)-trifluoroacetamide (CF(3)PAF). The antioxidant capacity of BSA and trolox has been assessed by measuring the amount of trifluoroacetamide (TFAM) arising from the radical mediated decomposition of CF(3)PAF. When assayed separately, both trolox and BSA behaved as antioxidants, as they were effective to protect CF(3)PAF from HO* radical-mediated decomposition. By contrast, trolox enhanced the production of TFAM in the presence of BSA, thus behaving as a pro-oxidant. Urate, carnosine, glucose, and propylgallate showed antioxidant properties both with or without BSA. CF(3)PAF and trolox were found to bind to BSA with association constants in the order of 5 x 10(3)M(-1) and to compete for the same binding sites. These results have been discussed in terms of BSA-catalysed cross-reactions between trolox-derived secondary radicals and CF(3)PAF. PMID:12878205

  14. Effects of the Interaction of Rifamycin SV with Serum Albumins on the Resonance Rayleigh Scattering Spectra and Their Analytical Application

    Institute of Scientific and Technical Information of China (English)

    YANG Ji-Dong; CAO Tuan-Wu; LIU Zhong-Fang; KONG Ling; LIU Shao-Pu

    2008-01-01

    In pH 4.5-4.8 Britton-Robinson buffer solution,rifamycin SV(i.e.rifamycin sodium)can react with serum albumin such as human selqlm albumin(HSA)and bovine serum albumin(BSA)to form macromolecular complexes by electrostatic attraction and hydrophobic force.As a result,the resonance Rayleigh scattering(RRS)of the drug was enhanced remarkably and the RRS peaks were at 374 and 552 nm.The enhancement of RRS(△I)is directly proportional to the concentration of HSA or BSA.The linear ranges and the detection limits are 0.03-6.0μg/mL and 9.0 ng/mL for HSA.and 0.01-8.0μg/mL and 2.0 ng/mL for BSA,respectively.In this work,a sensitive,selective,simple and fast methOd for the determination of trace amounts of serum albumin by RRS technique has been developed,which Was applied to the determination of serum albumin in the synthesized samples and human urine samples with satisfactory results.

  15. Amides complexing with BSA in presence of GuHCl; Kompleksowanie amidow z BSA w obecnosci GuHCl

    Energy Technology Data Exchange (ETDEWEB)

    Michnik, A.; Sulkowska, A. [Wydzial Farmaceutyczny, Slaska Akademia Medyczna, Sosnowiec (Poland)

    1994-12-31

    Mechanism of amides complexing with albumin has been studied by means of {sup 1}H NMR. The assessment of hydrogen bonds contribution in interaction of amides with albumin has been done through analysis of denaturation agent (GuHCl) influence results. 1 ref., 1 fig., 4 tabs.

  16. Interaction of cyclodextrins with human and bovine serum albumins: A combined spectroscopic and computational investigation

    Indian Academy of Sciences (India)

    Saptarshi Ghosh; Bijan Kumar Paul; Nitin Chattopadhyay

    2014-07-01

    Interaction of cyclodextrins (CDs) with the two most abundant proteins, namely human serum albumin (HSA) and bovine serum albumin (BSA), has been investigated using steady-state and time-resolved fluorometric techniques, circular dichroism measurements and molecular docking simulation. The study reveals that the three CDs interact differently on the fluorescence and fluorescence lifetimes of the serum albumins. However, fluorescence anisotropy and circular dichroism are not affected. Depending on their size, different CDs bind to the serum albumins in different positions, resulting in changes in the spectral behaviour of the proteins. Docking study suggests the probable binding sites of the three CDs with the proteins. Combined experimental and computational studies imply that sufficiently high concentration of CDs causes loosening of the rigid structures of these transport proteins, although their secondary structures remain intact. Thus, CDs are found to be safe for the serum proteins from the structural point of view.

  17. Controlled ultraviolet resonance energy transfer between bovine serum albumin donors and cadmium sulfide quantum dots acceptors

    Science.gov (United States)

    Ghali, Mohsen; El-Kemary, Maged; Ramadan, Mahmoud

    2015-08-01

    We report on Förester resonance nergy transfer (FRET) within a bioconjugated system composed of cadmium sulfide (CdS) quantum dots (QDs) and transport protein bovine serum albumin (BSA). The optical properties of these two elements of the bioconjugate were exploited to produce FRET in the ultraviolet (UV) region with a maximum efficiency of 22% from BSA donors to QD acceptors. In contrast to previous studies, which were limited to FRET in the visible light, we used 2.6 nm CdS QDs because they emit light with a shorter wavelength (∼370 nm) that facilitates the UV-FRET process. UV-FRET was controlled by tuning the spectral overlap between BSA and CdS QDs.

  18. Quenching of tryptophan fluorescence of bovine serum albumin under the effect of ions of heavy metals

    Science.gov (United States)

    Plotnikova, O. A.; Mel'nikov, A. G.; Mel'nikov, G. V.; Gubina, T. I.

    2016-01-01

    The interaction of heavy metals with bovine serum albumin (BSA) has been studied using data of quenching of intrinsic fluorescence of the protein by the ions of the heavy metals. Under the assumption of static quenching with formation of nonfluorescent complexes of fluorophores of BSA with heavy metals, conclusions have been drawn on the peculiarities of binding of the heavy metals to the protein. The values of the Stern-Volmer constants of association and those of the constants of BSA binding to the heavy metals decrease in the order Cu(II) > Pb(II) > Cd(II). It has been experimentally found that the copper ions have greater capacity to bind to the protein with the formation of the nonfluorescent complexes, which results in a significant decrease in the fluorescence intensity of the protein.

  19. Interaction of Palmitic Acid with Metoprolol Succinate at the Binding Sites of Bovine Serum Albumin

    Directory of Open Access Journals (Sweden)

    Mashiur Rahman

    2014-12-01

    Full Text Available Purpose: The aim of this study was to characterize the binding profile as well as to notify the interaction of palmitic acid with metoprolol succinate at its binding site on albumin. Methods: The binding of metoprolol succinate to bovine serum albumin (BSA was studied by equilibrium dialysis method (ED at 27°C and pH 7.4, in order to have an insight in the binding chemistry of the drug to BSA in presence and absence of palmitic acid. The study was carried out using ranitidine as site-1 and diazepam as site-2 specific probe. Results: Different analysis of binding of metoprolol succinate to bovine serum albumin suggested two sets of association constants: high affinity association constant (k1 = 11.0 x 105 M-1 with low capacity (n1 = 2 and low affinity association (k2 = 4.0×105 M-1 constant with high capacity (n2 = 8 at pH 7.4 and 27°C. During concurrent administration of palmitic acid and metoprolol succinate in presence or absence of ranitidine or diazepam, it was found that palmitic acid displaced metoprolol succinate from its binding site on BSA resulting reduced binding of metoprolol succinate to BSA. The increment in free fraction of metoprolol succinate was from 26.27% to 55.08% upon the addition of increased concentration of palmitic acid at a concentration of 0×10-5 M to 16×10-5 M. In presence of ranitidine and diazepam, palmitic acid further increases the free fraction of metoprolol succinate from 33.05% to 66.95% and 40.68% to 72.88%, respectively. Conclusion: This data provided the evidence of interaction at higher concentration of palmitic acid at the binding sites on BSA, which might change the pharmacokinetic properties of metoprolol succinate.

  20. A Novel Conductive Poly(3,4-ethylenedioxythiophene-BSA Film for the Construction of a Durable HRP Biosensor Modified with NanoAu Particles

    Directory of Open Access Journals (Sweden)

    Fangcheng Xu

    2016-03-01

    Full Text Available In this study, we have investigated the contribution of bovine serum albumin (BSA to the durability of the electrochemically synthesized poly(3,4-ethylenedioxythiophene (PEDOT film on a platinum (Pt electrode. The electrode was capable to effectively adsorb the nano Au particles (AuNPs to form a uniform layout, which was then able to immobilize the horseradish peroxidase (HRP to construct a functional HRP/AuNPs/PEDOT(BSA/Pt biosensor. Cyclic voltammetry was employed to evaluate the performance of the biosensor through the measurement of hydrogen peroxide. Our results revealed a satisfied linear correlation between the cathodic current and the concentration of H2O2. Furthermore, the addition of oxidized form of nicotinamide adenine dinucleotide, or NAD+, as the electron transfer mediator in the detection solution could dramatically enhance the sensitivity of detection by about 35.5%. The main advantages of the current biosensor are its durability, sensitivity, reliability, and biocompatibility.

  1. BSA-catalyzed Michael-aldol cascade reaction%牛血清蛋白催化Michael-Aldol串联反应的研究

    Institute of Scientific and Technical Information of China (English)

    王早; 刘晨江; 王吉德; 王娜

    2012-01-01

    首次报道了牛血清蛋白(BSA)催化二苯甲酰甲烷和丁烯酮的Michael-Aldol串联反应,并对1,3-二羰基化合物进行了研究,丁烯酮与α,β-不饱和酮酯化合物只生成一分子Michael及双分子Michael加成产物,该方法为合成环状化合物提供了新的途径.%Bovine serum albumin (BSA) was able to catalyse Michael-Aldol cascade reaction between MVK and dibenzoyl methane. Furthermore,we also studied other 1,3-dicarbonyl compounds, which gave one or two molecules Michael addition product. The method provided a new way to synthesize cyclic compounds

  2. Fluorescence spectroscopic studies on binding of a flavonoid antioxidant quercetin to serum albumins

    Indian Academy of Sciences (India)

    Beena Mishra; Atanu Barik; K Indira Priyadarsini; Hari Mohan

    2005-11-01

    Binding of quercetin to human serum albumin (HSA) was studied and the binding constant measured by following the red-shifted absorption spectrum of quercetin in the presence of HSA and the quenching of the intrinsic protein fluorescence in the presence of different concentrations of quercetin. Fluorescence lifetime measurements of HSA showed decrease in the average lifetimes indicating binding at a location, near the tryptophan moiety, and the possibility of fluorescence energy transfer between excited tryptophan and quercetin. Critical transfer distance () was determined, from which the mean distance between tryptophan-214 in HSA and quercetin was calculated. The above studies were also carried out with bovine serum albumin (BSA).

  3. Coupling of albumin flux to volume flow in skin and muscles of anesthetized rats

    International Nuclear Information System (INIS)

    Bovine serum albumin (BSA) labeled with 131I or 125I was injected intravenously in pentobarbital sodium-anesthetized rats, and tracer clearances into leg skin and muscles were measured over 30, 60, and 120 min. BSA labeled with the alternate tracer was used as vascular volume reference. Two minutes before injection of the tracer, a ligature was tied around one femoral vein to occlude outflow partially and raise capillary pressure in that leg. The unoccluded leg served as control. Skin and muscles of the occluded leg had variably and substantially higher water contents (delta W) than paired control tissues and slightly but consistently increased albumin clearances (CA). The delta CA/delta W, equivalent to the albumin concentration of capillary filtrate relative to plasma determined by linear regression, were as follows: leg skin 0.004 (95% confidence limits -0.001 to +0.009), muscle biceps femoris 0.005 (0.001-0.010), muscle gastrocnemius 0.011 (0.004-0.019), muscle tibialis anterior 0.016 (0.012-0.021). All these values are significantly less than 0.10, which corresponds to a reflection coefficient for serum albumin (sigma A) of 0.90. Convective coupling of albumin flux to volume flux in skin and muscles of intact, anesthetized rats is low, with sigma AS in the range 0.98 to greater than 0.99

  4. Preparation and Charaterization of Self-assembled Nanoparticles Based on Linolenic-acid Modified Chitosan

    Institute of Scientific and Technical Information of China (English)

    LIU Chenguang; Desai Kashappa Goud H.; CHEN Xiguang; Park Hyun-Jin

    2005-01-01

    Chitosan was modified by conjugating coupling with linolenic acid through the 1-ethyl-3-(3-dimethylaminopropyyl) earbodiimide (EDC)-mediated reaction. The degree of substitution 1.8% (i.e. 1.8 linolenic acid group per 100anhydroglucose units) was measured by 1H NMR. The critical aggregation concentration (CAC) of the self-aggregate of hydrophobically modified chitosan was determined by measuring the fluorescence intensity of the pyrene as a fluorescent probe.The CAC value in phosphate-buffered saline (PBS) solution (pH7.4) was 5 × 10-2 mgmL-1. The average particle size of selfaggregates of hydrophobically modified chitosan in PBS solution (pH7.4) was 210.8 nm with a unimodal size distribution ranging from 100 to 500 nm. Transmission electron microscopy (TEM) study showed that the formation of near spherical shape nanoparticles has enough structural integrity. The loading ability of hydrophibically modified chitosan (LA-chitosan)was investigated by using bovine serum albumin (BSA) as the model. The loading capacity of self-aggregated nanoparticles increases (19.85% ± 0.04% to 37.57% ± 0.25 %) with the concentration of BSA (0.1-0.5 mg mL-1).

  5. Investigating the colloidal stability of fluorescent silica nanoparticles under isotonic conditions for biomedical applications.

    Science.gov (United States)

    Nooney, Robert I; White, Angela; O'Mahony, Christy; O'Connell, Claire; Kelleher, Susan M; Daniels, Stephen; McDonagh, Colette

    2015-10-15

    Fluorescent silica nanoparticle (NP) labels are of great interest in biomedical diagnostics, however, when used in bioassays under physiological conditions they rapidly agglomerate and precipitate from solution leading to high levels of non-specific binding. In this work, using size and zeta-potential data obtained from Dynamic and Electrophoretic Light Scattering analysis, the improvement in colloidal stability of silica NPs under physiological conditions was correlated with an increase in the concentration of three additives: (1) a protein, bovine serum albumin (BSA); (2) a neutral surfactant, Tween 20®; and (3) a charged surfactant, sodium dodecyl sulfate (SDS). The number of BSA molecules present in the NP corona at each concentration was calculated using UV-Vis spectroscopy and a bicinchoninic acid protein assay (BCA). The optimal concentration of each additive was also effective in stabilizing antibody labeled fluorescent nanoparticles (αNPs) under physiological conditions. Using a fourth additive, trehalose, the colloidal stability of αNPs after freeze-drying and long-term storage also significantly improved. Both as-prepared and freeze-dried αNPs were tested in a standard fluorescence immunoassay for the detection of human IgG. The as-prepared assay showed a higher sensitivity at low concentration and a lower limit of detection when compared to a free dye assay. Assays performed with freeze dried αNPs after 4 and 22 days also showed good reproducibility. PMID:26092116

  6. Detection of Biomolecular Binding Through Enhancement of Localized Surface Plasmon Resonance (LSPR by Gold Nanoparticles

    Directory of Open Access Journals (Sweden)

    Min-Gon Kim

    2009-03-01

    Full Text Available To amplify the difference in localized surface plasmon resonance (LSPR spectra of gold nano-islands due to intermolecular binding events, gold nanoparticles were used. LSPR-based optical biosensors consisting of gold nano-islands were readily made on glass substrates using evaporation and heat treatment. Streptavidin (STA and biotinylated bovine serum albumin (Bio-BSA were chosen as the model receptor and the model analyte, respectively, to demonstrate the effectiveness of this detection method. Using this model system, we were able to enhance the sensitivity in monitoring the binding of Bio-BSA to gold nano-island surfaces functionalized with STA through the addition of gold nanoparticle-STA conjugates. In addition, SU-8 well chips with gold nano-island surfaces were fabricated through a conventional UV patterning method and were then utilized for image detection using the attenuated total reflection mode. These results suggest that the gold nano-island well chip may have the potential to be used for multiple and simultaneous detection of various bio-substances.

  7. Analysis of Bovine Serum Albumin Ligands from Puerariae flos Using Ultrafiltration Combined with HPLC-MS

    OpenAIRE

    Ping Tang; Shihui Si; Liangliang Liu

    2015-01-01

    Rapid screening techniques for identification of active compounds from natural products are important not only for clarification of the therapeutic material basis, but also for supplying suitable chemical markers for quality control. In the present study, ultrafiltration combined with high performance liquid chromatography-mass spectrometry (HPLC-MS) was developed and conducted to screen and identify bovine serum albumin (BSA) bound ligands from Puerariae flos. Fundamental parameters affectin...

  8. Sodium Alginate Microneedle Arrays Mediate the Transdermal Delivery of Bovine Serum Albumin

    OpenAIRE

    Yusuf K Demir; Zafer Akan; Oya Kerimoglu

    2013-01-01

    BACKGROUND: The "poke and release" strategy for the delivery of macromolecules using polymeric microneedle (MN) is of great importance because it eliminates microneedle reuse, the risks of biohazardous sharps and cross contamination, and it requires no special disposal mechanism. The main objective of this study was the determination of the stability and delivery of bovine serum albumin (BSA) that was transported across human skin via sodium alginate (SA) microneedle arrays (MNs) and SA needl...

  9. Investigation of the interaction of naringin palmitate with bovine serum albumin: spectroscopic analysis and molecular docking.

    Directory of Open Access Journals (Sweden)

    Xia Zhang

    Full Text Available BACKGROUND: Bovine serum albumin (BSA contains high affinity binding sites for several endogenous and exogenous compounds and has been used to replace human serum albumin (HSA, as these two compounds share a similar structure. Naringin palmitate is a modified product of naringin that is produced by an acylation reaction with palmitic acid, which is considered to be an effective substance for enhancing naringin lipophilicity. In this study, the interaction of naringin palmitate with BSA was characterised by spectroscopic and molecular docking techniques. METHODOLOGY/PRINCIPAL FINDINGS: The goal of this study was to investigate the interactions between naringin palmitate and BSA under physiological conditions, and differences in naringin and naringin palmitate affinities for BSA were further compared and analysed. The formation of naringin palmitate-BSA was revealed by fluorescence quenching, and the Stern-Volmer quenching constant (KSV was found to decrease with increasing temperature, suggesting that a static quenching mechanism was involved. The changes in enthalpy (ΔH and entropy (ΔS for the interaction were detected at -4.11 ± 0.18 kJ·mol(-1 and -76.59 ± 0.32 J·mol(-1·K(-1, respectively, which indicated that the naringin palmitate-BSA interaction occurred mainly through van der Waals forces and hydrogen bond formation. The negative free energy change (ΔG values of naringin palmitate at different temperatures suggested a spontaneous interaction. Circular dichroism studies revealed that the α-helical content of BSA decreased after interacting with naringin palmitate. Displacement studies suggested that naringin palmitate was partially bound to site I (subdomain IIA of the BSA, which was also substantiated by the molecular docking studies. CONCLUSIONS/SIGNIFICANCE: In conclusion, naringin palmitate was transported by BSA and was easily removed afterwards. As a consequence, an extension of naringin applications for use in food, cosmetic

  10. Investigations of acetaminophen binding to bovine serum albumin in the presence of fatty acid: Fluorescence and 1H NMR studies

    Science.gov (United States)

    Bojko, B.; Sułkowska, A.; Maciążek-Jurczyk, M.; Równicka, J.; Sułkowski, W. W.

    2009-04-01

    The binding of acetaminophen to bovine serum albumin (BSA) was studied by the quenching fluorescence method and the proton nuclear magnetic resonance technique ( 1H NMR). For fluorescence measurements 1-anilino-9-naphthalene sulfonate (ANS) hydrophobic probe was used to verify subdomain IIIA as acetaminophen's likely binding site. Three binding sites of acetaminophen in subdomain IIA of bovine serum albumin were found. Quenching constants calculated by the Stern-Volmer modified method were used to estimate the influence of myristic acid (MYR) on the drug binding to the albumin. The influence of [fatty acid]/[albumin] molar ratios on the affinity of the protein towards acetaminophen was described. Changes of chemical shifts and relaxation times of the drug indicated that the presence of MYR inhibits interaction in the AA-albumin complex. It is suggested that the elevated level of fatty acids does not significantly influence the pharmacokinetics of acetaminophen.

  11. Bovine serum albumin adsorption on functionalized porous silicon surfaces

    Science.gov (United States)

    Tay, Li-Lin; Rowell, Nelson L.; Lockwood, David J.; Boukherroub, Rabah

    2004-10-01

    The large surface area within porous Si (pSi) and its strong room temperature photoluminescence (PL) make it an ideal host for biological sensors. In particular, the development of pSi-based optical sensors for DNA, enzyme and other biochemical molecules have become of great interest. Here, we demonstrate that the in-situ monitoring of the pSi PL behaviour can be used as a positive identification of bovine serum albumin (BSA) protein adsorption inside the porous matrix. Electrochemically prepared pSi films were first functionalized with undecylenic acid to produce an organic monolayer covalently attached to the porous silicon surfaces. The acid terminal group also provided favourable BSA binding sites on the pSi matrix sidewalls. In-situ PL spectra showed a gradual red shift (up to 12 meV) in the PL peak energy due to the protein incorporation into the porous matrix. The PL then exhibited a continuous blue shift after saturation of the protein molecules in the pores. This blue shift of the PL peak frequency and a steady increase in the PL intensity is evidence of surface oxidation. Comparing the specular reflectance obtained by Fourier transform infrared spectroscopy (FTIR) before and after BSA incubation confirmed the adsorption of protein in the pSi matrix.

  12. Interactions between imazethapyr and bovine serum albumin: Spectrofluorimetric study

    International Nuclear Information System (INIS)

    The interaction between imazethapyr (IMA) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy. The Stern–Volmer quenching constant (KSV) at three temperatures was evaluated in order to determine the quenching mechanism. The dependence of fluorescence quenching on viscosity was also evaluated for this purpose. The results showed that IMA quenches the fluorescence intensity of BSA through a static quenching process. The values of the binding constant for the formed BSA–IMA complex and the number of binding sites were found to be 1.51×105 M−1 and 0.77, respectively, at room temperature. Based on the calculated thermodynamic parameters, the forces that dominate the binding process are hydrogen bonds and van der Waals forces, and the binding process is spontaneous and exothermic. The quenching of protein fluorescence by iodide ion was used to probe the accessibility of tryptophan residues in BSA and the change in accessibility induced by the presence of IMA. According to the obtained results, the BSA–IMA complex is formed in the site where the Trp-134 is located, causing it to become less exposed to the solvent. - Highlights: ► Fluorescence spectroscopy helps to understand protein binding mechanisms. ► Quenching measurements reveal the nature of the binding process involved. ► Iodine ion can be used to study the change in accessibility of tryptophan residues. ► Thermodynamic parameters for the binding reaction confirm binding modes.

  13. Spectroscopic and docking studies of the binding of two stereoisomeric antioxidant catechins to serum albumins

    Energy Technology Data Exchange (ETDEWEB)

    Roy, Durba; Dutta, Samrajnee; Maity, Shyam Sundar [Department of Chemistry, Presidency University, Kolkata 700 073 (India); Ghosh, Sanjib, E-mail: sanjibg@cal2.vsnl.net.in [Department of Chemistry, Presidency University, Kolkata 700 073 (India); Singha Roy, Atanu; Ghosh, Kalyan Sundar [Department of Chemistry, Indian Institute of Technology, Kharagpur 721 302 (India); Dasgupta, Swagata, E-mail: swagata@chem.iitkgp.ernet.in [Department of Chemistry, Indian Institute of Technology, Kharagpur 721 302 (India)

    2012-06-15

    The interactions of two stereoisomeric antioxidant flavonoids, catechin (C) and epicatechin (EC) with bovine serum albumin (BSA) and human serum albumin (HSA), have been investigated by steady state and time resolved fluorescence, phosphorescence, circular dichroism (CD), FTIR and protein-ligand docking studies. The steady-state fluorescence studies indicate a single binding site for both the ligands. FTIR spectra suggest that in both the albumins, C and EC stabilize the {alpha}-helix at the cost of a corresponding loss in the {beta}-sheet structure. CD studies have been carried out using ({+-})C, and both the epimers (+)C and (-)C. The low temperature phosphorescence and protein-ligand [(+), (-) and ({+-}) forms of C and EC] docking studies indicate that the ligands bind in the proximity of Trp 134 of BSA and Trp 214 of HSA, thereby changing their solvent accessible surface areas (ASA). Asn 158 and Glu 130 side chains are found to be within the hydrogen bonding distance from the phenolic -OH groups of C and EC in the case of BSA complex. C and EC are located within the binding pocket of sub-domain IIa of HSA. - Highlights: Black-Right-Pointing-Pointer Binding of two biologically important stereoisomeric antioxidants. Black-Right-Pointing-Pointer To find a significant role in pharmacology. Black-Right-Pointing-Pointer To find the conformational changes of the protein leading to the perturbation of Trp residues.

  14. Investigations into the oxygen effect during the radiolysis of serum albumin with the help of SDS-polyacrylamide gel electrophoresis

    International Nuclear Information System (INIS)

    In this work the radiation induced structural changes of serum albumin were researched with the help of SDS-polyacrylamide gel electrophoresis. Cow serum albumin (bSA) at a concentration of 1 mg/ml was dissolved in a solution of 10-2 M sodium phosphate buffer and in an air saturated solution with and without formiate (10-1 M) and irradiated with 200 kV X-rays up to doses of 1500 Gy in a nitrogen atmosphere. The irradiation products were separated, with and without reduction, to 7.5 and 10% polyacrylamide gel, their molecular weights measured and the quantitative decrease of the monomeric serum albumin with increasing dose estimated using staining methods. With increasing dose in an air atmosphere the amount of bSA decreases, after reduction even more so, and at least 14 different protein fragments whose molecular weights were determined result from this. In the formiate-containing solution a bSA decrease of up to 20% was observed, but only in the reduced solutions. The nitrogen atmosphere during the irradiation resulted in protein aggregate formation (2, 3 and 4 times the molecular weight of the monomeric bSA). Changes in the protein size, structure, and net charge as reasons for the electrophoretic behavior are discussed as well as the importance of the primary radicals during the radiation chemical reactions. (orig./RB)

  15. A fluorescence spectroscopic study of the interaction between Glipizide and bovine serum albumin and its analytical application

    International Nuclear Information System (INIS)

    The interaction between Glipizide and bovine serum albumin (BSA), as well as the effect of some metal ions (Zn2+, Cu2+, Mn2+, Mg2+, Ni2+, V5+, Cr6+, Mo6+) on the BSA–Glipizide system were investigated at different temperatures by fluorescence spectroscopy. Results showed that Glipizide could quench the intrinsic fluorescence of BSA, and the quenching mechanism was a dynamic quenching process. The hydrophobic force played an important role on the conjugation reaction between BSA and Glipizide. The binding constants (Ka) were 1.45×104, 3.09×104, 4.51×104 L/mol at 293, 303 and 310 K, respectively, and the number of binding site (n) in the binary system was approximate to 1. The binding distance (r) was about 2.80 nm and the primary binding for Glipizide was located at the structure domain II A of BSA. The synchronous fluorescence spectra and CD spectra revealed that the microenvironment and the conformation of BSA were changed during the binding reaction. A new method of using BSA as probe to determine the content of Glipizide by fluorescence spectroscopy was established, and it was applied to analysis of Glipizide in tablets with a satisfying result. -- Highlights: • Glipizide could quench the intrinsic fluorescence of BSA strongly. • Hydrophobic force played an important role on the conjugation reaction. • The order of magnitude of binding constants (Ka) was 104. • Synchronous spectra revealed that the conformation of BSA was changed. • CD spectra revealed that the conformation of BSA was also changed

  16. A fluorescence spectroscopic study of the interaction between Glipizide and bovine serum albumin and its analytical application

    Energy Technology Data Exchange (ETDEWEB)

    Cao, Shina; Liu, Baosheng, E-mail: lbs@hbu.edu.cn; Li, Zhiyun; Chong, Baohong

    2014-01-15

    The interaction between Glipizide and bovine serum albumin (BSA), as well as the effect of some metal ions (Zn{sup 2+}, Cu{sup 2+}, Mn{sup 2+}, Mg{sup 2+}, Ni{sup 2+}, V{sup 5+}, Cr{sup 6+}, Mo{sup 6+}) on the BSA–Glipizide system were investigated at different temperatures by fluorescence spectroscopy. Results showed that Glipizide could quench the intrinsic fluorescence of BSA, and the quenching mechanism was a dynamic quenching process. The hydrophobic force played an important role on the conjugation reaction between BSA and Glipizide. The binding constants (K{sub a}) were 1.45×10{sup 4}, 3.09×10{sup 4}, 4.51×10{sup 4} L/mol at 293, 303 and 310 K, respectively, and the number of binding site (n) in the binary system was approximate to 1. The binding distance (r) was about 2.80 nm and the primary binding for Glipizide was located at the structure domain II A of BSA. The synchronous fluorescence spectra and CD spectra revealed that the microenvironment and the conformation of BSA were changed during the binding reaction. A new method of using BSA as probe to determine the content of Glipizide by fluorescence spectroscopy was established, and it was applied to analysis of Glipizide in tablets with a satisfying result. -- Highlights: • Glipizide could quench the intrinsic fluorescence of BSA strongly. • Hydrophobic force played an important role on the conjugation reaction. • The order of magnitude of binding constants (K{sub a}) was 10{sup 4}. • Synchronous spectra revealed that the conformation of BSA was changed. • CD spectra revealed that the conformation of BSA was also changed.

  17. Single Particle Dynamic Imaging and Fe3+ Sensing with Bright Carbon Dots Derived from Bovine Serum Albumin Proteins

    Science.gov (United States)

    Yang, Qingxiu; Wei, Lin; Zheng, Xuanfang; Xiao, Lehui

    2015-12-01

    In this work, we demonstrated a convenient and green strategy for the synthesis of highly luminescent and water-soluble carbon dots (Cdots) by carbonizing carbon precursors, i.e., Bovine serum albumin (BSA) nanoparticles, in water solution. Without post surface modification, the as-synthesized Cdots exhibit fluorescence quantum yield (Q.Y.) as high as 34.8% and display superior colloidal stability not only in concentrated salt solutions (e.g. 2 M KCl) but also in a wide range of pH solutions. According to the FT-IR measurements, the Cdots contain many carboxyl groups, providing a versatile route for further chemical and biological functionalization. Through conjugation of Cdots with the transacting activator of transcription (TAT) peptide (a kind of cell penetration peptide (CPP)) derived from human immunodeficiency virus (HIV), it is possible to directly monitor the dynamic interactions of CPP with living cell membrane at single particle level. Furthermore, these Cdots also exhibit a dosage-dependent selectivity toward Fe3+ among other metal ions, including K+, Na+, Mg2+, Hg2+, Co2+, Cu2+, Pb2+ and Al3+. We believed that the Cdots prepared by this strategy would display promising applications in various areas, including analytical chemistry, nanomedicine, biochemistry and so on.