Spectroscopic characterization and docking studies of ZnO nanoparticle modified with BSA

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Ledesma, Ana E., E-mail: anael@unse.edu.ar [CITSE-UNSE, CONICET, FCEyT, RN 9, km 1125, 4206 Santiago del Estero (Argentina); Chemes, Doly María [INQUINOA, UNT, CONICET, FBQyF, San Lorenzo 456, San Miguel de Tucumán CPA T4000ILI, Tucumán (Argentina); Frías, María de los Angeles [Laboratory of Biointerphases and Biomimetic Systems, (CITSE) National University of Santiago del Estero and CONICET, 4206, RN 9- Km 1125, Santiago del Estero (Argentina); Guauque Torres, Maria del Pilar [CITSE-UNSE, CONICET, FCEyT, RN 9, km 1125, 4206 Santiago del Estero (Argentina)

2017-08-01

Highlights: • The ZnO NPs have synthesized at moderate temperature and conjugated with BSA to elucidate the characteristics of best binding site in the protein cavity. • The Docking studies have successfully applied to identify the amino acids residues involved in the interaction. • The cytotoxicity of ZnO NPs and ZnO-BSA NPs and esterase-like activity of the protein have evaluated, with very promising results for medical applications. - Abstract: Nanoparticles (NP) into a biological environment are an interesting topic for diagnosis and therapy in applications for medicine or environment and the knowledge about this interaction is important from the perspective of safe use of nanomaterials. In the current study, we characterized the type of interaction and the orientation of bovine serum albumin (BSA) adsorbed on ZnO nanoparticle surfaces as a function of size, using molecular docking. To probe experimentally different theoretical hypothesis about the interaction, ZnO-NPs were prepared in aqueous solution, and then were bioconjugated with BSA. Transmission electron microscopy (TEM) and Raman spectroscopy confirm the spherical shape of NP and the irreversible adsorption of BSA on NP surface. Raman and Infrared spectroscopy (FTIR) reveal that BSA interaction with ZnO nanoparticle produced a conformational rearrangement into protein, observing changes in Tyr and Trp environment, a minor percentage of α-helix structure and a more extended chain. The fluorescence analysis demonstrated that when BSA concentration higher than 30 μM is used the signal due to the self-oligomerization of protein overlaps with the ZnO nanoparticle emission. The results predicted that the most probable interaction site is near to domain IB and IIA and ionic interactions are the major responsible for the binding. Thermal stability studies reveals that the denaturalization temperature of BSA increase from 57 °C to 65 °C in presence of ZnO NP and their esterase-like activity was

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

International Nuclear Information System (INIS)

Chen, Zhi; Wu, Dudu

2012-01-01

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 (K q ). 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.

A DSC study of zinc binding to bovine serum albumin (BSA

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SANJA OSTOJIC

2007-04-01

Full Text Available The thermal denaturation of bovine serum albumin (BSA is a kinetically and thermodynamically controlled process. The effects of zinc binding to bovine serum albumin (BSA, followed by differential scanning calorimetry (DSC, were investigated in this work, with the purpose of obtaining a better understanding of the albumin/zinc interaction. From the DSC curves, the thermodynamic parameters of protein denaturation were obtained, i.e., the temperature of thermal transition maximum (Tm, calorimetric enthalpy (DHcal, van't Hoff enthalpy (DHvH, the number of binding sites (I, II, the binding constants for each binding site (KbI, KbII and the average number of ligands bound per mole of native protein XN. The thermodynamic data of protein unfolding showed that zinc binding to bovine serum albumin increases the stability of the protein (higher values of DHcal and the different ratio DHcal/DHvH indicates the perturbation of the protein during thermal denaturation.

Spectroscopic exploration of interaction between PEG-functionalized Ag2S nanoparticles with bovine serum albumin

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Prasanth, S.; RitheshRaj, D.; Vineeshkumar, T. V.; Sudarsanakumar, C.

2018-05-01

The introduction of nanoparticles into biological fluids often leads to the formation of biocorona over the surface of nanoparticles. For the effective use of nanoparticles in biological applications it is very essential to understand their interactions with proteins. Herein, we investigated the interactions of Poly ethylene glycol capped Ag2S nanoparticles with Bovine Serum Albumin by spectroscopic techniques. By the addition of Ag2S nanoparticles, a ground state complex is formed. The CD spectroscopy reveals that the secondary structure of BSA is altered by complexation with PEG-Ag2S nanoparticles, while the overall tertiary structure remains closer to that of native BSA.

Development of Acyclovir-Loaded Albumin Nanoparticles and Improvement of Acyclovir Permeation Across Human Corneal Epithelial T Cells.

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Suwannoi, Panita; Chomnawang, Mullika; Sarisuta, Narong; Reichl, Stephan; Müller-Goymann, Christel C

2017-12-01

The aim of the present study was to develop acyclovir (ACV) ocular drug delivery systems of bovine serum albumin (BSA) nanoparticles as well as to assess their in vitro transcorneal permeation across human corneal epithelial (HCE-T) cell multilayers. The ACV-loaded BSA nanoparticles were prepared by desolvation method along with physicochemical characterization, cytotoxicity, as well as in vitro transcorneal permeation studies across HCE-T cell multilayers. The nanoparticles appeared to be spherical in shape and nearly uniform in size of about 200 nm. The size of nanoparticles became smaller with decreasing BSA concentration, while the ratios of water to ethanol seemed not to affect the size. Increasing the amount of ethanol in desolvation process led to significant reduction of drug entrapment of nanoparticles with smaller size and more uniformity. The ACV-loaded BSA nanoparticles prepared were shown to have no cytotoxic effect on HCE-T cells used in permeation studies. The in vitro transcorneal permeation results revealed that ACV could permeate through the HCE-T cell multilayers significantly higher from BSA nanoparticles than from aqueous ACV solutions. The ACV-loaded BSA nanoparticles could be prepared by desolvation method without glutaraldehyde in the formulation. ACV could increasingly permeate through the multilayers of HCE-T cells from the ACV-loaded BSA nanoparticles. Therefore, the ACV-loaded BSA nanoparticles could be a highly potential ocular drug delivery system.

Reducing agent-free synthesis of curcumin-loaded albumin nanoparticles by self-assembly at room temperature.

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Safavi, Maryam Sadat; Shojaosadati, Seyed Abbas; Yang, Hye Gyeong; Kim, Yejin; Park, Eun Ji; Lee, Kang Choon; Na, Dong Hee

2017-08-30

The purpose of this study was to prepare curcumin-loaded bovine serum albumin nanoparticles (CCM-BSA-NPs) by reducing agent-free self-assembly at room temperature. A 2 4 factorial design approach was used to investigate the CCM-BSA-NP preparation process at different pH values, temperatures, dithiothreitol amounts, and CCM/BSA mass ratios. Increasing the ionic strength enabled preparation of CCM-BSA-NPs at 25°C without reducing agent. CCM-BSA-NPs prepared under the optimized conditions at 25°C showed a particle size of 110±6nm, yield of 88.5%, and drug loading of 7.1%. The CCM-BSA-NPs showed strong antioxidant activity and neuroprotective effects in glutamate-induced mouse hippocampal neuronal HT22 cells. This study suggests that ionic strength can be a key parameter affecting the preparation of albumin-based NPs. Copyright © 2017 Elsevier B.V. All rights reserved.

Synthesis and characterization of folate decorated albumin bio-conjugate nanoparticles loaded with a synthetic curcumin difluorinated analogue.

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Gawde, Kaustubh A; Kesharwani, Prashant; Sau, Samaresh; Sarkar, Fazlul H; Padhye, Subhash; Kashaw, Sushil K; Iyer, Arun K

2017-06-15

Albumin-bound paclitaxel colloidal nanoparticle (Abraxane®) is an FDA approved anticancer formulation available in the market. It is a suspension which is currently used therapeutically for treating cancers of the breast, lung, and pancreas among others. CDF is a novel new and potent synthetic curcumin analogue that is widely used for breast and ovarian cancer. The aim of this study was to use biocompatible albumin as well as folate decorated albumin to formulate colloidal nanoparticles encapsulating curcumin difluorinated (CDF). CDF has demonstrated a 16-fold improvement in stability and remarkable anticancer potency compared to its natural derivative, curcumin. CDF showed marked inhibition of cancer cell growth through down-regulation of multiple miRNAs, up-regulation of phosphatase and tensin homolog (PTEN), and attenuation of histone methyl transferase EZH2. However, CDF is highly hydrophobic and photodegradable with sparing aqueous solubility. In this study, we have formulated albumin nanoparticle using a modified desolvation method, which yielded high CDF loading in a nanoformulation. The physicochemical properties of CDF loaded albumin and folate-decorated albumin nanosuspensions were assessed for particle size, morphology, zeta potential, drug encapsulation efficiency/loading, solubility and drug release. Importantly, the folate ligand decorated albumin nanoparticles were formulated in principle to passively and actively target folate-overexpressing-cancers. In this study, the synthesis and optimization of BSA and folate decorated BSA conjugated CDF nanoparticles are assessed in detail that will be useful for its future clinical translation. Copyright © 2017 Elsevier Inc. All rights reserved.

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.

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.

Electrophoretic properties of BSA-coated quantum dots.

Science.gov (United States)

Bücking, Wendelin; Massadeh, Salam; Merkulov, Alexei; Xu, Shu; Nann, Thomas

2010-02-01

Low toxic InP/ZnS quantum dots (QDs), ZnS:Mn(2+)/ZnS nanocrystals and CdSe/ZnS nanoparticles were rendered water-dispersible by different ligand-exchange methods. Eventually, they were coated with bovine serum albumin (BSA) as a model protein. All particles were characterised by isotachophoresis (ITP), laser Doppler velocimetry (LDV) and agarose gel electrophoresis. It was found that the electrophoretic mobility and colloidal stability of ZnS:Mn(2+)/ZnS and CdSe/ZnS nanoparticles, which bore short-chain surface ligands, was primarily governed by charges on the nanoparticles, whereas InP/ZnS nanocrystals were not charged per se. BSA-coated nanoparticles showed lower electrophoretic mobility, which was attributed to their larger size and smaller overall charge. However, these particles were colloidally stable. This stability was probably caused by steric stabilisation of the BSA coating.

Development and characterization of glutathione-conjugated albumin nanoparticles for improved brain delivery of hydrophilic fluorescent marker.

Science.gov (United States)

Patel, Prerak J; Acharya, Niyati S; Acharya, Sanjeev R

2013-01-01

The glutathione-conjugated bovine serum albumin (BSA) nanoparticles were constructed in the present exploration as a novel biodegradable carrier for brain-specific drug delivery with evaluation of its in vitro and in vivo delivery properties. BSA nanocarriers were activated and conjugated to the distal amine functions of the glutathione via carbodiimide chemistry using EDAC as a mediator. These nanoparticles were characterized for particle shape, average size, SPAN value, drug entrapment and in vitro drug release. Further, presence of glutathione on the surface of BSA nanoparticles was confirmed by Ellman's assay, which has suggested that approximately 750 units of glutathione were conjugated per BSA nanoparticle. To evaluate the brain delivery properties of the glutathione-conjugated BSA nanoparticles fluorescein sodium was used as a model hydrophilic compound. Permeability and neuronal uptake properties of developed formulations were evaluated against the MDCK-MDR1 endothelial and neuro-glial cells, respectively. The permeability of glutathione-conjugated BSA nanoparticles across the monolayer of MDCK-MDR1 endothelial tight junction was shown significantly higher than that of unconjugated nanoparticles and fluorescein sodium solution. Similarly, glutathione-conjugated nanoparticles exhibited considerably higher uptake by neuro-glial cells which was inferred by high fluorescence intensity under microscope in comparison to unconjugated nanoparticles and fluorescein sodium solution. Following an intravenous administration, nearly three folds higher fluorescein sodium was carried to the rat brain by glutathione-conjugated nanoparticles as compared to unconjugated nanoparticles. The significant in vitro and in vivo results suggest that glutathione-conjugated BSA nanoparticles is a promising brain drug delivery system with low toxicity.

Effect of bovine serum albumin (BSA) on enzymatic cellulose hydrolysis.

Science.gov (United States)

Wang, Hui; Mochidzuki, Kazuhiro; Kobayashi, Shinichi; Hiraide, Hatsue; Wang, Xiaofen; Cui, Zongjun

2013-06-01

Bovine serum albumin (BSA) was added to filter paper during the hydrolysis of cellulase. Adding BSA before the addition of the cellulase enhances enzyme activity in the solution, thereby increasing the conversion rate of cellulose. After 48 h of BSA treatment, the BSA adsorption quantities are 3.3, 4.6, 7.8, 17.2, and 28.3 mg/g substrate, each with different initial BSA concentration treatments at 50 °C; in addition, more cellulase was adsorbed onto the filter paper at 50 °C compared with 35 °C. After 48 h of hydrolysis, the free-enzyme activity could not be measured without the BSA treatment, whereas the remaining activity of the filter paper activity was approximately 41 % when treated with 1.0 mg/mL BSA. Even after 96 h of hydrolysis, 25 % still remained. Meanwhile, after 48 h of incubation without substrate, the remaining enzyme activities were increased 20.7 % (from 43.7 to 52.7 %) and 94.8 % (from 23.3 to 45.5 %) at 35 and 50 °C, respectively. Moreover, the effect of the BSA was more obvious at 35 °C compared with 50 °C. When using 15 filter paper cellulase units per gram substrate cellulase loading at 50 °C, the cellulose conversion was increased from 75 % (without BSA treatment) to ≥90 % when using BSA dosages between 0.1 and 1.5 mg/mL. Overall, these results suggest that there are promising strategies for BSA treatment in the reduction of enzyme requirements during the hydrolysis of cellulose.

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)

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

International Nuclear Information System (INIS)

Leal, Jessica; Silva, Andressa A.; Geraldes, Adriana N.; Lugao, Ademar B.; Grasselli, Mariano

2015-01-01

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 4 salt to AuNPs performed by gamma radiation 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)

Residual bovine serum albumin (BSA) quantitation in vaccines using automated Capillary Western technology.

Science.gov (United States)

Loughney, John W; Lancaster, Catherine; Ha, Sha; Rustandi, Richard R

2014-09-15

Bovine serum albumin (BSA) is a major component of fetal bovine serum (FBS), which is commonly used as a culture medium during vaccine production. Because BSA can cause allergic reactions in humans the World Health Organization (WHO) has set a guidance of 50 ng or less residual BSA per vaccine dose. Vaccine manufacturers are expected to develop sensitive assays to detect residual BSA. Generally, sandwich enzyme-linked immunosorbent assays (ELISA) are used in the industry to detect these low levels of BSA. We report the development of a new improved method for residual BSA detection using the SimpleWestern technology to analyze residual BSA in an attenuated virus vaccine. The method is based on automated Capillary Western and has linearity of two logs, >80% spike recovery (accuracy), intermediate precision of CV <15%, and LOQ of 5.2 ng/ml. The final method was applied to analyze BSA in four lots of bulk vaccine products and was used to monitor BSA clearance during vaccine process purification. Copyright © 2014 Elsevier Inc. All rights reserved.

Biomimetic synthesis of hybrid hydroxyapatite nanoparticles using nanogel template for controlled release of bovine serum albumin.

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Qin, Jinli; Zhong, Zhenyu; Ma, Jun

2016-05-01

A biomimetic method was used to prepare hybrid hydroxyapatite (HAP) nanoparticles with chitosan/polyacrylic acid (CS-PAA) nanogel. The morphology, structure, crystallinity, thermal properties and biocompatibility of the obtained hybrid nanogel-HAP nanoparticles have been characterized. In addition, bovine serum albumin (BSA) was used as a model protein to study the loading and release behaviors of the hybrid nanogel-HAP nanoparticles. The results indicated that the obtained HAP nanoparticles were agglomerated and the nanogel could regulate the formation of HAP. When the nanogel concentration decreased, different HAP crystal shapes and agglomerate structures were obtained. The loading amount of BSA reached 67.6 mg/g for the hybrid nanoparticles when the mineral content was 90.4%, which decreased when the nanogel concentration increased. The release profile of BSA was sustained in neutral buffer. Meanwhile, an initial burst release was found at pH 4.5 due to the desorption of BSA from the surface, followed by a slow release. The hemolysis percentage of the hybrid nanoparticles was close to the negative control, and these particles were non-toxic to bone marrow stromal stem cells. The results suggest that these hybrid nanogel-HAP nanoparticles are promising candidate materials for biocompatible drug delivery systems. Copyright © 2016 Elsevier B.V. All rights reserved.

Gold nanoparticles as a factor of influence on doxorubicin-bovine serum albumin complex

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Goncharenko, N. A.; Pavlenko, O. L.; Dmytrenko, O. P.; Kulish, M. P.; Lopatynskyi, A. M.; Chegel, V. I.

2018-04-01

The interaction between doxorubicin (Dox) and bovine serum albumin (BSA) complex with gold nanoparticles (AuNPs) was investigated by optical spectroscopy. The optical absorption of Dox and BSA solutions was studied. The formation of Dox-BSA complexes with a binding constant K = 7.56 × 106 M-2 and the number of binding sites n = 2 was found out. With pH 6.9, the concentration of complexes is an order of magnitude lower than the concentration of unbound antibiotic molecules. Optical absorption in solutions of Dox-BSA conjugates in the presence of AuNPs undergoes a significant rearrangement, which manifests the changes in the magnitude of the hydrophobic interaction of BSA with Dox, changes in the conformational state of antibiotic, and, as a consequence, a plasmon-induced change in the mechanism of complex formation. The aggregation of the Dox-AuNPs conjugate depends on the presence and concentration of BSA and in the case of formation of the Dox-BSA complex is minimal.

Albumin and Hyaluronic Acid-Coated Superparamagnetic Iron Oxide Nanoparticles Loaded with Paclitaxel for Biomedical Applications

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Elena Vismara

2017-06-01

Full Text Available Super paramagnetic iron oxide nanoparticles (SPION were augmented by both hyaluronic acid (HA and bovine serum albumin (BSA, each covalently conjugated to dopamine (DA enabling their anchoring to the SPION. HA and BSA were found to simultaneously serve as stabilizing polymers of Fe3O4·DA-BSA/HA in water. Fe3O4·DA-BSA/HA efficiently entrapped and released the hydrophobic cytotoxic drug paclitaxel (PTX. The relative amount of HA and BSA modulates not only the total solubility but also the paramagnetic relaxation properties of the preparation. The entrapping of PTX did not influence the paramagnetic relaxation properties of Fe3O4·DA-BSA. Thus, by tuning the surface structure and loading, we can tune the theranostic properties of the system.

Fluorescence spectral studies on interaction of fluorescent probes with Bovine Serum Albumin (BSA)

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Ghosh, Kaushik, E-mail: ghoshfcy@iitr.ac.in; Rathi, Sweety; Arora, Deepshikha

2016-07-15

Interaction of 2-(1-(naphthale-1-ylimino)ethyl)phenol (1), 2-methoxy-4-(((4-methoxyphenyl)imino)methyl)phenol (2) and 2-methoxy-4-((naphthalene-1-ylimino)methyl)phenol (3) with Bovine Serum Albumin (BSA) was examined. Fluorescence spectral data were obtained from the probes by varying the concentration of BSA as well as from BSA by varying the concentration of probes. Synchronous fluorescence measurements were performed and binding constants of the probes were calculated. To understand mode of quenching, Stern–Volmer plot, absorption spectral studies and life time measurements were performed. Förster resonance energy transfer (FRET) was also scrutinized. - Highlights: • Schiff bases with pendant phenolato function and interaction with BSA. • Synchronous fluorescence studies and a preferred interaction with tryptophan. • Probable interaction of probes with Trp-213 residue in the hydrophobic cavity. • 1:1 binding stoichiometry of probes and BSA in Benesi–Hildebrand graph.

Doxorubicin hinders DNA condensation promoted by the protein bovine serum albumin (BSA).

Science.gov (United States)

Lima, C H M; de Paula, H M C; da Silva, L H M; Rocha, M S

2017-12-01

In this work, we have studied the interaction between the anticancer drug doxorubicin (doxo) and condensed DNA, using optical tweezers. To perform this task, we use the protein bovine serum albumin (BSA) in the working buffer to mimic two key conditions present in the real intracellular environment: the condensed state of the DNA and the abundant presence of charged macromolecules in the surrounding medium. In particular, we have found that, when doxo is previously intercalated in disperse DNA, the drug hinders the DNA condensation process upon the addition of BSA in the buffer. On the other hand, when bare DNA is firstly condensed by BSA, doxo is capable to intercalate and to unfold the DNA condensates at relatively high concentrations. In addition, a specific interaction between BSA and doxo was verified, which significantly changes the chemical equilibrium of the DNA-doxo interaction. Finally, the presence of BSA in the buffer stabilizes the double-helix structure of the DNA-doxo complexes, preventing partial DNA denaturation induced by the stretching forces. © 2017 Wiley Periodicals, Inc.

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

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.

Immune responses induced in rabbits after oral administration of bovine serum albumin in combination with different adjuvants (herb extracts, aluminium hydroxide and platinum nanoparticles

Directory of Open Access Journals (Sweden)

G. Bižanov

2016-12-01

Full Text Available The aim of the current study was to evaluate the immunostimulatory activity of 10 different herbal extracts from Vitex agnus-castus, Vinca major, Aloe arborescens and the polyherbal product containing extracts from Sambucus nigra, Primula versis, Pinus alba, Gentiana lutea, Cetraria islandica, Eucaliptus globulus, Citrus limon and aluminium hydroxide, as well as platinum nanoparticles. Rabbits were immunized three times orally with bovine serum albumin (BSA in combination with the components mentioned above. BSA-specific IgA antibodies in saliva and IgG antibodies in serum were examined by ELISA. It was found that the rabbits immunized with BSA in combination with either platinum nanoparticles or aluminium hydroxide had higher titres of BSA-specific IgA antibodies in their saliva at day 56 of observation. Likewise, rabbits treated with BSA and Vinca major or Aloe arborescens extracts showed higher levels of BSA-specific IgG antibodies in the serum at the end of observation. These results suggest that some plant extracts, aluminium hydroxide and platinum nanoparticles components could be used as oral adjuvants or as immunomodulators for rabbits.

Preparation of magnetic albumin nanoparticles via a simple and one-pot desolvation and co-precipitation method for medical and pharmaceutical applications.

Science.gov (United States)

Nosrati, Hamed; Salehiabar, Marziyeh; Manjili, Hamidreza Kheiri; Danafar, Hossein; Davaran, Soodabeh

2018-03-01

In this study, iron oxide magnetic bovine serum albumin core-shell nanoparticles (BSA coated IONPs) with narrow particle size distribution were synthesized under one-pot reaction via the desolvation and chemical co-precipitation method. Functionalized IONPs were characterized by X-ray diffraction (XRD), differential scanning calorimetry (DSC), thermogravimetric analysis (TGA), fourier transform infrared spectroscopy (FTIR), and transmission electron microscopy (TEM) techniques. Furthermore, vibrating sample magnetometer (VSM) analysis show these nanoparticles (NPs) have an excellent magnetic properties. Cellular toxicity of IONPs was also investigated on HFF2 cell lines. Additionally, a hemolysis test of as prepared core-shell NPs were performed. The presence of albumin as a biomolecule coating on the surface of IONPs showed an improving effect to reduce the cytotoxicity. The properties of the designed NPs propose the BSA coated IONPs as a promising candidate for multifunctional biomedical applications. Copyright © 2017 Elsevier B.V. All rights reserved.

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)

Gu, Yu; Li, Nan; Gao, Mengmeng; Wang, Zilu; Xiao, Deli; Li, Yun; Jia, Huning; He, Hua

2015-01-01

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)

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.

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

International Nuclear Information System (INIS)

Chen, Dandan; Xie, Jinhui; Wu, Qiong; Fan, Ping; Wang, Jun

2015-01-01

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

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

Synthetic nanoparticles of bovine serum albumin with entrapped salicylic acid

Directory of Open Access Journals (Sweden)

Bronze-Uhle ES

2016-12-01

Full Text Available ES Bronze-Uhle,1 BC Costa,1 VF Ximenes,2 PN Lisboa-Filho1 1Department of Physics, São Paulo State University (Unesp, School of Sciences, Bauru, São Paulo, Brazil; 2Department of Chemistry, São Paulo State University (Unesp, School of Sciences, Bauru, São Paulo, Brazil Abstract: Bovine serum albumin (BSA is highly water soluble and binds drugs or inorganic substances noncovalently for their effective delivery to various affected areas of the body. Due to the well-defined structure of the protein, containing charged amino acids, albumin nanoparticles (NPs may allow electrostatic adsorption of negatively or positively charged molecules, such that substantial amounts of drug can be incorporated within the particle, due to different albumin-binding sites. During the synthesis procedure, pH changes significantly. This variation modifies the net charge on the surface of the protein, varying the size and behavior of NPs as the drug delivery system. In this study, the synthesis of BSA NPs, by a desolvation process, was studied with salicylic acid (SA as the active agent. SA and salicylates are components of various plants and have been used for medication with anti-inflammatory, antibacterial, and antifungal properties. However, when administered orally to adults (usual dose provided by the manufacturer, there is 50% decomposition of salicylates. Thus, there has been a search for some time to develop new systems to improve the bioavailability of SA and salicylates in the human body. Taking this into account, during synthesis, the pH was varied (5.4, 7.4, and 9 to evaluate its influence on the size and release of SA of the formed NPs. The samples were analyzed using field-emission scanning electron microscopy, transmission electron microscopy, Fourier transform infrared, zeta potential, and dynamic light scattering. Through fluorescence, it was possible to analyze the release of SA in vitro in phosphate-buffered saline solution. The results of

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. Copyright © 2015 John Wiley & Sons, Ltd.

Preparation, characterization and cytotoxic evaluation of bovine serum albumin nanoparticles encapsulating 5-methylmellein: A secondary metabolite isolated from Xylaria psidii.

Science.gov (United States)

Arora, Divya; Kumar, Amit; Gupta, Prasoon; Chashoo, Gousia; Jaglan, Sundeep

2017-12-01

In this study, 5-methylmellein (5-MM) loaded bovine serum albumin nanoparticles (BSA NPs) were developed using desolvation technique. The developed nanoparticles were characterized for their mean particle size, polydispersity, zeta potential, loading efficiency, X-ray diffractometry (XRD), differential scanning calorimetry (DSC) and release profile. The developed nanoparticles were spherical in shape under transmission electron microscopy (TEM) and atomic force microscopy (AFM). The developed 5-MM loaded BSA NPs demonstrated a mean particle size with a diameter of 154.95 ± 4.44 nm. The results from XRD and DSC studies demonstrated that the crystal state of the 5-MM was converted to an amorphous state in polymeric matrix. The encapsulation and loading efficiency was found to be 73.26 ± 4.48% and 7.09 ± 0.43%. The in vitro cytotoxicity in human prostate cancer cell line (PC-3), human colon cancer cells (HCT-116) and human breast adenocarcinoma cell line (MCF-7) cells demonstrated enhanced cytotoxicity of 5-MM BSA NPs as compared to native 5-MM after 72-h treatment. The enhancement in cytotoxicity of 5-MM BSA NPs was also supported by increase in cellular apoptosis, mitochondrial membrane potential loss and generation of high reactive oxygen species (ROS). In conclusion, these findings collectively indicated that BSA nanoparticles may serve as promising drug delivery system for improving the efficacy of 5-methylmellein. Copyright © 2017 Elsevier Ltd. All rights reserved.

Probing into the binding interaction between medroxyprogesterone acetate and bovine serum albumin (BSA): spectroscopic and molecular docking methods.

Science.gov (United States)

Fang, Fang; Pan, Dong-Qi; Qiu, Min-Jie; Liu, Ting-Ting; Jiang, Min; Wang, Qi; Shi, Jie-Hua

2016-09-01

To further understand the mechanism of action and pharmacokinetics of medroxyprogesterone acetate (MPA), the binding interaction of MPA with bovine serum albumin (BSA) under simulated physiological conditions (pH 7.4) was studied using fluorescence emission spectroscopy, synchronous fluorescence spectroscopy, circular dichroism and molecular docking methods. The experimental results reveal that the fluorescence of BSA quenches due to the formation of MPA-BSA complex. The number of binding sites (n) and the binding constant for MPA-BSA complex are ~1 and 4.6 × 10(3)  M(-1) at 310 K, respectively. However, it can be concluded that the binding process of MPA with BSA is spontaneous and the main interaction forces between MPA and BSA are van der Waals force and hydrogen bonding interaction due to the negative values of ΔG(0) , ΔH(0) and ΔS(0) in the binding process of MPA with BSA. MPA prefers binding on the hydrophobic cavity in subdomain IIIA (site II'') of BSA resulting in a slight change in the conformation of BSA, but BSA retaining the α-helix structure. Copyright © 2016 John Wiley & Sons, Ltd. Copyright © 2016 John Wiley & Sons, Ltd.

Physicochemical characterization of 3,6-diHydroxyflavone binding BSA immobilized on PEG-coated silver nanoparticles

Energy Technology Data Exchange (ETDEWEB)

Voicescu, Mariana, E-mail: voicescu@icf.ro [Institute of Physical Chemistry “Ilie Murgulescu” of the Romanian Academy (Romania); Ionescu, Sorana [University of Bucharest, Department of Physical Chemistry (Romania); Calderon-Moreno, Jose M. [Institute of Physical Chemistry “Ilie Murgulescu” of the Romanian Academy (Romania); Nistor, Cristina L. [National R& D Institute for Chemistry and Petrochemistry ICECHIM, Polymer Department (Romania)

2017-02-15

Studies based on silver nanoparticles (SNPs) and polyethylene glycols (PEGs) are mainly in the pharmaceutical field, with PEG as good “vehicle” to transport protein-based drugs. In this work, physicochemical characteristics of 3,6-diHydroxyflavone (3,6-diHF) binding bovine serum albumin (BSA) on PEG (Tween20, L64, and Myrj52)-coated SNPs have been investigated by steady-state and time-resolved fluorescence spectroscopy. These interactions give rise to the formation of intermolecular and intramolecular H bonds. As a subject of interest, the effect of temperature (30–60 °C) on the H bonds was studied by steady-state fluorescence. The size distribution and zeta potential of SNPs were determined by dynamic light scattering (DLS). Scanning electron microscopy (SEM) analysis revealed the spherical nature of particles with average diameter ~40–80 nm. The structure, stability, dynamics, and conformational changes in adsorbed BSA protein on the PEG-coated SNPs surface have been also investigated by steady-state/lifetime fluorescence and circular dichroism spectroscopy. The results have relevance in the oxidative stress and drug delivery processes.

Physicochemical characterization of 3,6-diHydroxyflavone binding BSA immobilized on PEG-coated silver nanoparticles

Science.gov (United States)

Voicescu, Mariana; Ionescu, Sorana; Calderon-Moreno, Jose M.; Nistor, Cristina L.

2017-02-01

Studies based on silver nanoparticles (SNPs) and polyethylene glycols (PEGs) are mainly in the pharmaceutical field, with PEG as good "vehicle" to transport protein-based drugs. In this work, physicochemical characteristics of 3,6-diHydroxyflavone (3,6-diHF) binding bovine serum albumin (BSA) on PEG (Tween20, L64, and Myrj52)-coated SNPs have been investigated by steady-state and time-resolved fluorescence spectroscopy. These interactions give rise to the formation of intermolecular and intramolecular H bonds. As a subject of interest, the effect of temperature (30-60 °C) on the H bonds was studied by steady-state fluorescence. The size distribution and zeta potential of SNPs were determined by dynamic light scattering (DLS). Scanning electron microscopy (SEM) analysis revealed the spherical nature of particles with average diameter 40-80 nm. The structure, stability, dynamics, and conformational changes in adsorbed BSA protein on the PEG-coated SNPs surface have been also investigated by steady-state/lifetime fluorescence and circular dichroism spectroscopy. The results have relevance in the oxidative stress and drug delivery processes.

Spectroscopic analyses on interaction of bovine serum albumin (BSA) with toluidine blue (TB) and its sonodynamic damage under ultrasonic irradiation

Energy Technology Data Exchange (ETDEWEB)

Wang Jun, E-mail: wangjun890@126.co [Department of Chemistry, Liaoning University, Shenyang 110036 (China); Guo Yuwei [Department of Chemistry, Liaoning University, Shenyang 110036 (China); Department of Chemistry, Baotou Normal College, Baotou 014030 (China); Liu Bin [Department of Pharmacy, Liaoning University, Shenyang 110036 (China); Cheng Chunping [Department of Chemistry, Baotou Normal College, Baotou 014030 (China); Wang Zhiqiu; Han Guangxi; Gao Jingqun; Zhang Xiangdong [Department of Chemistry, Liaoning University, Shenyang 110036 (China)

2011-02-15

In this paper, the toluidine blue (TB) with tricyclic quinone imide plane structure is used as sonosensitizer to study the interaction and sonodynamic damage to bovine serum albumin (BSA) by UV-vis and fluorescence spectroscopy. The results show that the TB can bind to BSA molecules, obviously, and the synergetic effects of TB and ultrasonic irradiation can efficiently damage the BSA molecules. Otherwise, some influencing factors such as ultrasonic irradiation time, TB concentration, pH value and ionic strength on the damage of BSA molecules were also considered by the numbers. Synchronous fluorescence spectroscopy indicates that the tyrosine (Tyr) residues of BSA molecules are damaged more seriously than the tryptophan (Trp) residues under ultrasonic irradiation. - Research Highlights: TB is used as quencher to study interaction to BSA. TB is used as sonosensitizer to study the sonodynamic damage to BSA. Synchronous fluorescence spectroscopy is used to study TB binding site to BSA.

Synthesis and characterization of magnetite nanoparticles having different cover layer and investigation of cover layer effect on the adsorption of lysozyme and bovine serum albumin.

Science.gov (United States)

Shah, Muhammad Tariq; Alveroglu, Esra

2017-12-01

In this study, differently coated superparamagnetic Fe 3 O 4 (magnetite) nanoparticles were synthesized, characterized and used for lysozyme (Ly) and bovine serum albumin (BSA) adsorption. SiO 2 , carbon nanotubes (CNTs) and graphene were used for covering the readily synthesized magnetite nanoparticles to elucidate the effect of cover layer on the protein adsorption kinetics and capacities of nanostructure. XRD, FTIR, AFM, SEM, VSM and fluorescence measurements were used for the characterization of the samples and investigating the adsorption kinetics of Ly and BSA by these nanoparticles. The average particle size of the Fe 3 O 4 nanoparticles are approximately found as 10nm and VSM measurement shows that the Fe 3 O 4 particles have superparamagnetic behavior with no hysteresis and remnant. The adsorption kinetic of proteins on nanosized material is followed via fluorescence method. All the nanostructures with different cover layers obey pseudo first order kinetics and SiO 2 coated nanoparticles show the fastest kinetics and capabilities for Ly and BSA adsorption. Copyright © 2017 Elsevier B.V. All rights reserved.

Intermolecular interaction of fosinopril with bovine serum albumin (BSA): The multi-spectroscopic and computational investigation.

Science.gov (United States)

Zhou, Kai-Li; Pan, Dong-Qi; Lou, Yan-Yue; Shi, Jie-Hua

2018-04-16

The intermolecular interaction of fosinopril, an angiotensin converting enzyme inhibitor with bovine serum albumin (BSA), has been investigated in physiological buffer (pH 7.4) by multi-spectroscopic methods and molecular docking technique. The results obtained from fluorescence and UV absorption spectroscopy revealed that the fluorescence quenching mechanism of BSA induced by fosinopril was mediated by the combined dynamic and static quenching, and the static quenching was dominant in this system. The binding constant, K b , value was found to lie between 2.69 × 10 3 and 9.55 × 10 3  M -1 at experimental temperatures (293, 298, 303, and 308 K), implying the low or intermediate binding affinity between fosinopril and BSA. Competitive binding experiments with site markers (phenylbutazone and diazepam) suggested that fosinopril preferentially bound to the site I in sub-domain IIA on BSA, as evidenced by molecular docking analysis. The negative sign for enthalpy change (ΔH 0 ) and entropy change (ΔS 0 ) indicated that van der Waals force and hydrogen bonds played important roles in the fosinopril-BSA interaction, and 8-anilino-1-naphthalenesulfonate binding assay experiments offered evidence of the involvements of hydrophobic interactions. Moreover, spectroscopic results (synchronous fluorescence, 3-dimensional fluorescence, and Fourier transform infrared spectroscopy) indicated a slight conformational change in BSA upon fosinopril interaction. Copyright © 2018 John Wiley & Sons, Ltd.

Spectroscopic analyses on interaction of bovine serum albumin (BSA) with toluidine blue (TB) and its sonodynamic damage under ultrasonic irradiation

International Nuclear Information System (INIS)

Wang Jun; Guo Yuwei; Liu Bin; Cheng Chunping; Wang Zhiqiu; Han Guangxi; Gao Jingqun; Zhang Xiangdong

2011-01-01

In this paper, the toluidine blue (TB) with tricyclic quinone imide plane structure is used as sonosensitizer to study the interaction and sonodynamic damage to bovine serum albumin (BSA) by UV-vis and fluorescence spectroscopy. The results show that the TB can bind to BSA molecules, obviously, and the synergetic effects of TB and ultrasonic irradiation can efficiently damage the BSA molecules. Otherwise, some influencing factors such as ultrasonic irradiation time, TB concentration, pH value and ionic strength on the damage of BSA molecules were also considered by the numbers. Synchronous fluorescence spectroscopy indicates that the tyrosine (Tyr) residues of BSA molecules are damaged more seriously than the tryptophan (Trp) residues under ultrasonic irradiation. - Research Highlights: → TB is used as quencher to study interaction to BSA. → TB is used as sonosensitizer to study the sonodynamic damage to BSA. → Synchronous fluorescence spectroscopy is used to study TB binding site to BSA.

Binding interaction of ramipril with bovine serum albumin (BSA): Insights from multi-spectroscopy and molecular docking methods.

Science.gov (United States)

Shi, Jie-Hua; Pan, Dong-Qi; Jiang, Min; Liu, Ting-Ting; Wang, Qi

2016-11-01

The binding interaction between a typical angiotensin-converting enzyme inhibitor (ACEI), ramipril, and a transport protein, bovine serum albumin (BSA), was studied in vitro using UV-vis absorption spectroscopy, steady-state fluorescence spectroscopic titration, synchronous fluorescence spectroscopy, three dimensional fluorescence spectroscopy, circular dichroism and molecular docking under the imitated physiological conditions (pH=7.4). The experimental results suggested that the intrinsic fluorescence of BSA was quenched by ramipril thought a static quenching mechanism, indicating that the stable ramipril-BSA complex was formed by the intermolecular interaction. The number of binding sites (n) and binding constant of ramipril-BSA complex were about 1 and 3.50×10 4 M -1 at 298K, respectively, suggesting that there was stronger binding interaction of ramipril with BSA. The thermodynamic parameters together with molecular docking study revealed that both van der Waal's forces and hydrogen bonding interaction dominated the formation of the ramipril-BSA complex and the binding interaction of BSA with ramipril is enthalpy-driven processes due to |ΔH°|>|TΔS°| and ΔG°<0. The spatial distance between ramipril and BSA was calculated to be 3.56nm based on Förster's non-radiative energy transfer theory. The results of the competitive displacement experiments and molecular docking confirmed that ramipril inserted into the subdomain IIA (site I) of BSA, resulting in a slight change in the conformation of BSA but BSA still retained its secondary structure α-helicity. Copyright © 2016 Elsevier B.V. All rights reserved.

The role of nanoparticles in the albumin-cytarabine and albumin-methotrexate interactions

Energy Technology Data Exchange (ETDEWEB)

Pentak, Danuta, E-mail: danuta.pentak@us.edu.pl [Department of Materials Chemistry and Chemical Technology, Institute of Chemistry, University of Silesia, Szkolna 9, 40-006 Katowice (Poland); Maciążek-Jurczyk, Małgorzata; Zawada, Zygmunt H. [School of Pharmacy with the Division of Laboratory Medicine in Sosnowiec, Medical University of Silesia, Department of Physical Pharmacy, Jagiellońska 4, 41-200 Sosnowiec (Poland)

2017-04-01

Understanding the interactions which occur between nanomaterials and biomolecules is one of the most important issues in nanotechnology. Determining the properties of nanoparticles obtained through the use of novel methods and defining the scope of their application as drug carriers has important practical significance. Nanoparticles containing methotrexate and cytarabine obtained by a modified reverse-phase evaporation method (mREV) were characterized through the use of the UV/Vis and NMR methods. Obtained results confirmed high degree of analysed drugs encapsulation. The encapsulation efficiencies of cytarabine (AraC) and methotrexate (MTX) in L{sub DPPC/AraC/MTX} were found to be 86.30% (AraC) and 86.00% (MTX). The increased permeability of the phospholipid membranes, resulting from physico-chemical properties and the location of the drug, as well as from the physico-chemical properties of the phospholipids themselves, has been confirmed by increase in the length of the T1 relaxation time of protons in the −N{sup +}(CH{sub 3}){sub 3} group. The study of analysed drugs release process from the liposomes has been made for bovine serum albumin, both in the absence (dBSA) and in the presence of fatty acid (BSA). Moreover two types of kinetic models (Bhaskar equation and Rigter-Peppas equation) have been used. Based on the study it has been concluded that mathematical modelling of drug release can be very helpful in speeding up product development and in better understanding the mechanisms controlling drug release from advanced delivery systems. - Graphical abstract: In vitro drug release profiles of different liposomal formulation. - Highlights: • Liposomes containing tested drugs can be obtained by mREV method. • High degree of encapsulation characterizes obtained liposomes. • Cytarabine and methotrexate release from liposomes followed both: diffusion and controlled mechanisms.

Construction and evaluation of BSA-CaP nanomaterials with enhanced transgene performance via biocorona-inspired caveolae-mediated endocytosis

Science.gov (United States)

Ma, Xi-Xi; Gao, Han; Zhang, Ya-Xuan; Jia, Yi-Yang; Li, Chen; Zhou, Si-Yuan; Zhang, Bang-Le

2018-02-01

Non-viral nanovectors have attracted much attention owing to their ability to condense genetic materials and their ease of modification. However, their poor stability, low biocompatibility and gene degradation in endosomes or lysosomes has significantly hampered their application in vivo and in the clinic. In an attempt to overcome these difficulties a series of bovine serum albumin (BSA)-calcium phosphate (CaP) nanoparticles were constructed. The CaP condenses with DNA to form nanocomplexes coated with a biomimetic corona of BSA. Such complexes may retain the inherent endocytosis profile of BSA, with improved biocompatibility. In particular the transgene performance may be enhanced by stimulating the cellular uptake pathway via caveolae-mediated endocytosis. Two methods were employed to construct and optimize the formulation of BSA-CaP nanomaterials. The optimized BSA-CaP-50-M2 nanoparticles prepared by our second method exhibited good stability, negligible cytotoxicity and enhanced transgene performance with long-term expression for 72 h in vivo even with a single dose. Determination of the cellular uptake pathway and Western blot revealed that cellular uptake of the designed BSA-CaP-50-M2 nanoparticles was mainly via caveolae-mediated endocytosis in a non-degradative pathway in which the biomimetic uptake profile of BSA was retained.

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

International Nuclear Information System (INIS)

Ni, Yuyang; Li, Jun; Huang, Zhenzhen; He, Ke; Zhuang, Jiaqi; Yang, Wensheng

2013-01-01

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

Prodrug encapsulated albumin nanoparticles as an alternative approach to manifest anti-proliferative effects of suicide gene therapy

International Nuclear Information System (INIS)

Tirkey, Bulbul; Bhushan, Bharat; Uday Kumar, S.; Gopinath, P.

2017-01-01

Conventional anticancer agents are associated with limited therapeutic efficacy and substantial nonspecific cytotoxicity. Thus, there is an imminent need for an alternative approach that can specifically annihilate the cancer cells with minimal side effects. Among such alternative approaches, CD::UPRT (cytosine deaminase uracil phosphoribosyl transferase) suicide gene therapy has tremendous potential due to its high efficacy. Prodrug 5-Fluorocytosine (5-FC) used in combination with CD::UPRT suicide gene suffers from limited solubility which subsequently leads to decline in therapeutic efficacy. In order to overcome this, 5-FC encapsulated bovine serum albumin nanoparticles (BSA-5-FC NPs) were prepared in this work by desolvation method. Physico-chemical characterizations studies revealed amorphous nature of BSA-5-FC NPs with uniform spherical morphology. Apart from increase in solubility, encapsulated 5-FC followed slow and sustained release profile. Suicide gene expressing stable clone of L-132 cells were adapted for investigating therapeutic potential of BSA-5-FC NPs. These nanoparticles were readily taken up by the cells in a concentration dependent manner and subsequently manifested apoptosis, which was further confirmed by morphological examination and gene expression analysis. These findings clearly illustrate that CD::UPRT suicide gene therapy can be efficiently utilized in combination with this nanosystem for improved suicide gene therapy and tumor eradication. - Highlights: • In this work, BSA-5-FC NPs has been prepared to achieve its sustained release and also facilitate its uptake by cells. • A protein based system has been realized for the first time to deliver prodrug for cancer therapy. • Physico-chemical characterizations further validate the formation of spherical, monodispersed and stable nanoparticles. • The therapeutic efficacy of BSA-5-FC NPs has been validated against CD::UPRT expressing stable cells.

Prodrug encapsulated albumin nanoparticles as an alternative approach to manifest anti-proliferative effects of suicide gene therapy

Energy Technology Data Exchange (ETDEWEB)

Tirkey, Bulbul [Nanobiotechnology Laboratory, Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667 (India); Bhushan, Bharat; Uday Kumar, S. [Nanobiotechnology Laboratory, Centre for Nanotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667 (India); Gopinath, P., E-mail: pgopifnt@iitr.ernet.in [Nanobiotechnology Laboratory, Centre for Nanotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667 (India); Nanobiotechnology Laboratory, Department of Biotechnology, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand 247667 (India)

2017-04-01

Conventional anticancer agents are associated with limited therapeutic efficacy and substantial nonspecific cytotoxicity. Thus, there is an imminent need for an alternative approach that can specifically annihilate the cancer cells with minimal side effects. Among such alternative approaches, CD::UPRT (cytosine deaminase uracil phosphoribosyl transferase) suicide gene therapy has tremendous potential due to its high efficacy. Prodrug 5-Fluorocytosine (5-FC) used in combination with CD::UPRT suicide gene suffers from limited solubility which subsequently leads to decline in therapeutic efficacy. In order to overcome this, 5-FC encapsulated bovine serum albumin nanoparticles (BSA-5-FC NPs) were prepared in this work by desolvation method. Physico-chemical characterizations studies revealed amorphous nature of BSA-5-FC NPs with uniform spherical morphology. Apart from increase in solubility, encapsulated 5-FC followed slow and sustained release profile. Suicide gene expressing stable clone of L-132 cells were adapted for investigating therapeutic potential of BSA-5-FC NPs. These nanoparticles were readily taken up by the cells in a concentration dependent manner and subsequently manifested apoptosis, which was further confirmed by morphological examination and gene expression analysis. These findings clearly illustrate that CD::UPRT suicide gene therapy can be efficiently utilized in combination with this nanosystem for improved suicide gene therapy and tumor eradication. - Highlights: • In this work, BSA-5-FC NPs has been prepared to achieve its sustained release and also facilitate its uptake by cells. • A protein based system has been realized for the first time to deliver prodrug for cancer therapy. • Physico-chemical characterizations further validate the formation of spherical, monodispersed and stable nanoparticles. • The therapeutic efficacy of BSA-5-FC NPs has been validated against CD::UPRT expressing stable cells.

Small-angle neutron scattering study of differences in phase behavior of silica nanoparticles in the presence of lysozyme and bovine serum albumin proteins

Science.gov (United States)

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

2014-03-01

The differences in phase behavior of anionic silica nanoparticles (88 Å) in the presence of two globular proteins [cationic lysozyme (molecular weight (MW) 14.7 kD) and anionic bovine serum albumin (BSA) (MW 66.4 kD)] have been studied by small-angle neutron scattering. The measurements were carried out on a fixed concentration (1 wt %) of Ludox silica nanoparticles with varying concentrations of proteins (0-5 wt %) at pH = 7. It is found that, despite having different natures (opposite charges), both proteins can render to the same kind of aggregation of silica nanoparticles. However, the concentration regions over which the aggregation is observed are widely different for the two proteins. Lysozyme with very small amounts (e.g., 0.01 wt %) leads to the aggregation of silica nanoparticles. On the other hand, silica nanoparticles coexist with BSA as independent entities at low protein concentrations and turn to aggregates at high protein concentrations (>1 wt %). In the case of lysozyme, the charge neutralization by the protein on the nanoparticles gives rise to the protein-mediated aggregation of the nanoparticles. The nanoparticle aggregates coexist with unaggregated nanoparticles at low protein concentrations, whereas, they coexist with a free protein at higher protein concentrations. For BSA, the nonadsorbing nature of the protein produces the depletion force that causes the aggregation of the nanoparticles at higher protein concentrations. The evolution of the interaction is modeled by the two Yukawa potential, taking account of both attractive and repulsive terms of the interaction in these systems. The nanoparticle aggregation is found to be governed by the short-range attraction for lysozyme and the long-range attraction for BSA. The aggregates are characterized by the diffusion limited aggregate type of mass fractal morphology.

Spectroscopic and molecular docking approaches for investigating conformation and binding characteristics of clonazepam with bovine serum albumin (BSA).

Science.gov (United States)

Lou, Yan-Yue; Zhou, Kai-Li; Pan, Dong-Qi; Shen, Jia-Le; Shi, Jie-Hua

2017-02-01

Clonazepam, a type of benzodiazepine, is a classical drug used to prevent and treat seizures, panic disorder, movement disorder, among others. For further clarifying the distribution of clonazepam in vivo and the pharmacodynamic and pharmacokinetic mechanisms, the binding interaction between clonazepam and bovine serum albumin (BSA) was investigated using ultraviolet spectroscopy (UV), steady-state fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional (3D) fluorescence spectroscopy, Fourier transform infrared spectroscopy (FT-IR) and molecular docking methods. The results well confirmed that clonazepam bound on the subdomain III A (Site II) of BSA through van der Waals force and hydrogen bonding interaction, and quenched the intrinsic fluorescence of BSA through a static quenching process. The number of binding sites (n) and binding constant (K b ) of clonazepam-BSA complex were about 1 and 7.94×10 4 M -1 at 308K, respectively. The binding process of clonazepam with BSA was spontaneous and enthalpy-driven process due to ΔG 0 T|ΔS 0 | over the studied temperature range. Meanwhile, the binding interaction of clonazepam with BSA resulted in the slight change in the conformation of BSA and the obvious change in the conformation of clonazepam, implying that the flexibility of clonazepam also played an important role in increasing the stability of the clonazepam-BSA complex. Copyright © 2016 Elsevier B.V. All rights reserved.

Spectroscopic studies on the interaction and sonodynamic damage of neutral red (NR) to bovine serum albumin (BSA)

Energy Technology Data Exchange (ETDEWEB)

Liu Bin; Guo Ying [Department of Pharmacy, Liaoning University, Shenyang 110036 (China); Wang, Jun, E-mail: wangjun890@126.co [Department of Chemistry, Liaoning University, Shenyang 110036 (China); Xu Rui [Department of Chemistry, Liaoning University, Shenyang 110036 (China); Wang Xin; Wang Dan; Zhang Liqun [Department of Pharmacy, Liaoning University, Shenyang 110036 (China); Xu Yongnan [Department of Pharmacy, Shenyang Pharmaceutical University, Shenyang 110016 (China)

2010-06-15

In this paper, the interaction of neutral red (NR) with bovine serum albumin (BSA) and the sonodynamic damage to BSA under ultrasonic irradiation was studied by means of ultraviolet-visible (UV-vis) and fluorescence spectra. The quenching constant (K{sub SV}=5.749x10{sup 4} L/mol), binding constant (K{sub A}=3.19x10{sup 4} L/mol) and binding site number (n=0.9462) were measured. The binding distance (r=2.47 nm) between NR and BSA was obtained according to Foester's non-radiative energy transfer theory. The damage process of BSA molecules was detected by the hyperchromic effect of UV-vis spectra and quenching of intrinsic fluorescence spectra. In addition, the influencing factors such as ultrasonic irradiation time and NR concentration on the damage to BSA molecules were also considered. The results showed that the damage degree is enhanced with the increase of ultrasonic irradiation time and NR concentration. The possible mechanism of sonodynamic damage to BSA molecules was mainly mediated by singlet oxygen ({sup 1}O{sub 2}). Otherwise, the binding and damaging sites to BSA molecules were also estimated by synchronous fluorescence. The results indicated that the NR is more vicinal to tryptophan (Trp) residue than to tyrosine (Tyr) residue and the damage site is also mainly at Trp residues. The research result will bring a certain significance to use sonosensitive drugs in the fields of tumor treatment.

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

Characterizing the binding interaction between antimalarial artemether (AMT) and bovine serum albumin (BSA): Spectroscopic and molecular docking methods.

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Shi, Jie-Hua; Pan, Dong-Qi; Wang, Xiou-Xiou; Liu, Ting-Ting; Jiang, Min; Wang, Qi

2016-09-01

Artemether (AMT), a peroxide sesquiterpenoides, has been widely used as an antimalarial for the treatment of multiple drug-resistant strains of plasmodium falciparum malaria. In this work, the binding interaction of AMT with bovine serum albumin (BSA) under the imitated physiological conditions (pH7.4) was investigated by UV spectroscopy, fluorescence emission spectroscopy, synchronous fluorescence spectroscopy, Fourier transform infrared spectroscopy (FT-IR), circular dichroism (CD), three-dimensional fluorescence spectroscopy and molecular docking methods. The experimental results indicated that there was a change in UV absorption of BSA along with a slight red shift of absorption wavelength, indicating that the interaction of AMT with BSA occurred. The intrinsic fluorescence of BSA was quenched by AMT due to the formation of AMT-BSA complex. The number of binding sites (n) and binding constant of AMT-BSA complex were about 1 and 2.63×10(3)M(-1) at 298K, respectively, suggesting that there was stronger binding interaction of AMT with BSA. Based on the analysis of the signs and magnitudes of the free energy change (ΔG(0)), enthalpic change (ΔH(0)) and entropic change (ΔS(0)) in the binding process, it can be concluded that the binding of AMT with BSA was enthalpy-driven process due to |ΔH°|>|TΔS°|. The results of experiment and molecular docking confirmed the main interaction forces between AMT and BSA were van der Waals force. And, there was a slight change in the BSA conformation after binding AMT but BSA still retains its secondary structure α-helicity. However, it had been confirmed that AMT binds on the interface between sub-domain IIA and IIB of BSA. Copyright © 2016 Elsevier B.V. All rights reserved.

In vitro study on binding interaction of quinapril with bovine serum albumin (BSA) using multi-spectroscopic and molecular docking methods.

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Shi, Jie-Hua; Pan, Dong-Qi; Jiang, Min; Liu, Ting-Ting; Wang, Qi

2017-08-01

The binding interaction between quinapril (QNPL) and bovine serum albumin (BSA) in vitro has been investigated using UV absorption spectroscopy, steady-state fluorescence spectroscopic, synchronous fluorescence spectroscopy, 3D fluorescence spectroscopy, Fourier transform infrared spectroscopy, circular dichroism, and molecular docking methods for obtaining the binding information of QNPL with BSA. The experimental results confirm that the quenching mechanism of the intrinsic fluorescence of BSA induced by QNPL is static quenching based on the decrease in the quenching constants of BSA in the presence of QNPL with the increase in temperature and the quenching rates of BSA larger than 10 10  L mol -1  s -1 , indicating forming QNPL-BSA complex through the intermolecular binding interaction. The binding constant for the QNPL-BSA complex is in the order of 10 5  M -1 , indicating there is stronger binding interaction of QNPL with BSA. The analysis of thermodynamic parameters together with molecular docking study reveal that the main binding forces in the binding process of QNPL with BSA are van der Waal's forces and hydrogen bonding interaction. And, the binding interaction of BSA with QNPL is an enthalpy-driven process. Based on Förster resonance energy transfer, the binding distance between QNPL and BSA is calculated to be 2.76 nm. The results of the competitive binding experiments and molecular docking confirm that QNPL binds to sub-domain IIA (site I) of BSA. It is confirmed there is a slight change in the conformation of BSA after binding QNPL, but BSA still retains its secondary structure α-helicity.

Multifunctional BSA-Au nanostars for photoacoustic imaging and X-ray computed tomography.

Science.gov (United States)

Zu, Lihui; Liu, Lin; Qin, Yeshan; Liu, Hongguang; Yang, Haishan

2016-10-01

We report the synthesis and characterization of bovine serum albumin-capped Au nanostars (BSA-AuNSs) for dual-modal computed tomography (CT)/photoacoustic (PA) imaging application. The BSA-AuNSs have an average size of 85nm, and a surface plasmon resonance (SPR) peak at approximately 770nm. They have excellent biocompatibility, good X-ray attenuation, and great PA contrast enhancement properties. When injected intravenously, liver signal markedly increases in both CT and PA modalities. The in vivo biodistribution studies and pathology results showed that the BSA-AuNSs were mainly excreted through the liver and intestines with no obvious biotoxicity. These results indicate that BSA-AuNSs have high potential to be used as dual-modal CT/PA imaging contrast agents or further used to develop targeted probes. This preliminary study suggests that PA tomography may be used to non-invasively trace the kinetics and biodistribution of the nanoparticles. Copyright © 2016 Elsevier Inc. All rights reserved.

Electrochemical deposition of mineralized BSA/collagen coating

Energy Technology Data Exchange (ETDEWEB)

Zhuang, Junjun [School of Materials Science and Engineering, State Key Laboratory of Silicon Materials, Zhejiang University, Hangzhou 310027 (China); Lin, Jun; Li, Juan; Wang, Huiming [The First Affiliated Hospital of Medical College, Zhejiang University, Hangzhou 310003 (China); Cheng, Kui [School of Materials Science and Engineering, State Key Laboratory of Silicon Materials, Zhejiang University, Hangzhou 310027 (China); Weng, Wenjian, E-mail: wengwj@zju.edu.cn [School of Materials Science and Engineering, State Key Laboratory of Silicon Materials, Zhejiang University, Hangzhou 310027 (China); The Shanghai Institute of Ceramics, Chinese Academy of Sciences, Shanghai 200050 (China)

2016-09-01

In this work, mineralized collagen coatings with different loading quantity of bovine serum albumin (BSA) were prepared via in situ electrochemical deposition on titanium substrate. The microstructure and BSA loading quantity of the coatings could be controlled by the electrochemical deposition parameters, such as deposition potential, BSA concentration and its adding sequence in the electrolyte. The BSA loading quantity in the coatings was obtained in the range of 0.0170–0.173 mg/cm{sup 2}, enhancing the cell adhesion and proliferation of the coatings with the simultaneous release. The distinct release behaviors of BSA were attributed to their gradient distribution with different mineralization degrees, which could be adjusted by the deposition process. These results suggest that in situ electrochemical deposition is a promising way to incorporate functional molecules into the mineralized collagen coatings and the mineralized BSA/collagen coatings are highly promising for improving the rhBMP-2 loading capability (1.8-fold). - Highlights: • BSA is incorporated into mineralized collagen coating by electrochemical deposition. • The loading amount of BSA in coatings can be adjusted in the range of 0-173 ng. • The BSA/collagen coating shows good cytocompatibility with free-albumin culture. • The incorporation process is put forward for some other molecules deposition.

Spectroscopic investigation on assisted sonocatalytic damage of bovine serum albumin (BSA) by metronidazole (MTZ) under ultrasonic irradiation combined with nano-sized ZnO

Science.gov (United States)

Gao, Jingqun; Liu, Bin; Wang, Jun; Jin, Xudong; Jiang, Renzheng; Liu, Lijun; Wang, Baoxin; Xu, Yongnan

2010-11-01

The previous work proved that the bovine serum albumin (BSA) could be damaged under the combined action of ultrasonic irradiation and ZnO. In this work, the assisted sonocatalytic damage of BSA using metronidazole (MTZ) as a sensitizer was further investigated by means of UV-vis and fluorescence spectra. The results indicated that the adding of MTZ could obviously promote the sonocatalytic damage of BSA under ultrasonic irradiation in the presence of nano-sized ZnO powder. Furthermore, it was found that the damage degree of BSA was aggravated by some influencing factors except ionic kind and strength. In addition, the damage site of BSA was also studied with synchronous fluorescence technology. It was found that the damage site was mainly at tryptophan (Trp) residue.

Synthesis and characterization of dipicolinate sensitized LaF3:Tb3+ nanoparticles and their interaction with bovine serum albumin

International Nuclear Information System (INIS)

Jing, Kui; Guo, Xingjia; Diao, Xin; Wu, Qiong; Jiang, Yuchun; Sun, Ye; Pan, Xintong; Zhou, Nannan; Zhu, Yanjun

2015-01-01

Dipicolinate sensitized LaF 3 :Tb 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 4 L mol −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 3 :Tb 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

Storage Stabilisation of Albumin-Loaded Chitosan Nanoparticles by ...

African Journals Online (AJOL)

The rate of BSA leakage from the nanoparticles containing trehalose was reduced from 92 ... water. CS/DS nanoparticles were simultaneously prepared by adding 4 ml of DS solution dropwise ... performed in triplicate at 25 oC with a detection.

Interaction of Flavonoids from Woodwardia unigemmata with Bovine Serum Albumin (BSA): Application of Spectroscopic Techniques and Molecular Modeling Methods.

Science.gov (United States)

Ma, Rui; Pan, Hong; Shen, Tao; Li, Peng; Chen, Yanan; Li, Zhenyu; Di, Xiaxia; Wang, Shuqi

2017-08-09

Phytochemical investigation on the methanol extract of Woodwardia unigemmata resulted in the isolation of seven flavonoids, including one new flavonol acylglycoside ( 1 ). The structures of these compounds were elucidated on the basis of extensive spectroscopic analysis and comparison of literature data. The multidrug resistance (MDR) reversing activity was evaluated for the isolated compounds using doxorubicin-resistant K562/A02 cells model. Compound 6 showed comparable MDR reversing effect to verapamil. Furthermore, the interaction between compounds and bovine serum albumin (BSA) was investigated by spectroscopic methods, including steady-state fluorescence, synchronous fluorescence, circular dichroism (CD) spectroscopies, and molecular docking approach. The experimental results indicated that the seven flavonoids bind to BSA by static quenching mechanisms. The negative ΔH and ΔS values indicated that van der Waals interactions and hydrogen bonds contributed in the binding of compounds 2 - 6 to BSA. In the case of compounds 1 and 7 systems, the hydrophobic interactions play a major role. The binding of compounds to BSA causes slight changes in the secondary structure of BSA. There are two binding sites of compound 6 on BSA and site I is the main site according to the molecular docking studies and the site marker competitive binding assay.

The Interactions between ZnO Nanoparticles (NPs and α-Linolenic Acid (LNA Complexed to BSA Did Not Influence the Toxicity of ZnO NPs on HepG2 Cells

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Yiwei Zhou

2017-04-01

Full Text Available Background: Nanoparticles (NPs entering the biological environment could interact with biomolecules, but little is known about the interaction between unsaturated fatty acids (UFA and NPs. Methods: This study used α-linolenic acid (LNA complexed to bovine serum albumin (BSA for UFA and HepG2 cells for hepatocytes. The interactions between BSA or LNA and ZnO NPs were studied. Results: The presence of BSA or LNA affected the hydrodynamic size, zeta potential, UV-Vis, fluorescence, and synchronous fluorescence spectra of ZnO NPs, which indicated an interaction between BSA or LNA and NPs. Exposure to ZnO NPs with the presence of BSA significantly induced the damage to mitochondria and lysosomes in HepG2 cells, associated with an increase of intracellular Zn ions, but not intracellular superoxide. Paradoxically, the release of inflammatory cytokine interleukin-6 (IL-6 was decreased, which indicated the anti-inflammatory effects of ZnO NPs when BSA was present. The presence of LNA did not significantly affect all of these endpoints in HepG2 cells exposed to ZnO NPs and BSA. Conclusions: the results from the present study indicated that BSA-complexed LNA might modestly interact with ZnO NPs, but did not significantly affect ZnO NPs and BSA-induced biological effects in HepG2 cells.

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

Science.gov (United States)

Zaloga, Jan; Stapf, Marcus; Nowak, Johannes; Pöttler, Marina; Friedrich, Ralf P; Tietze, Rainer; Lyer, Stefan; Lee, Geoffrey; Odenbach, Stefan; Hilger, Ingrid; Alexiou, Christoph

2015-08-14

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 SEON(LA-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 SEON(LA-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 SEON(LA-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.

BSA Nanoparticles for siRNA Delivery: Coating Effects on Nanoparticle Properties, Plasma Protein Adsorption, and In Vitro siRNA Delivery

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Haran Yogasundaram

2012-01-01

Full Text Available Developing vehicles for the delivery of therapeutic molecules, like siRNA, is an area of active research. Nanoparticles composed of bovine serum albumin, stabilized via the adsorption of poly-L-lysine (PLL, have been shown to be potentially inert drug-delivery vehicles. With the primary goal of reducing nonspecific protein adsorption, the effect of using comb-type structures of poly(ethylene glycol (1 kDa, PEG units conjugated to PLL (4.2 and 24 kDa on BSA-NP properties, apparent siRNA release rate, cell viability, and cell uptake were evaluated. PEGylated PLL coatings resulted in NPs with ζ-potentials close to neutral. Incubation with platelet-poor plasma showed the composition of the adsorbed proteome was similar for all systems. siRNA was effectively encapsulated and released in a sustained manner from all NPs. With 4.2 kDa PLL, cellular uptake was not affected by the presence of PEG, but PEG coating inhibited uptake with 24 kDa PLL NPs. Moreover, 24 kDa PLL systems were cytotoxic and this cytotoxicity was diminished upon PEG incorporation. The overall results identified a BSA-NP coating structure that provided effective siRNA encapsulation while reducing ζ-potential, protein adsorption, and cytotoxicity, necessary attributes for in vivo application of drug-delivery vehicles.

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

International Nuclear Information System (INIS)

Zhou, Rui; Dong, Xueyan; Song, Lanlan; Jing, Hao

2014-01-01

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 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 2 O (9.0×10 4 )>NaCl (2.64×10 4 )/PBS (2.37×10 4 )>PBS-NaCl (0.88×10 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 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 2 O were smaller than that in three buffer solutions, which correlated with stronger binding force between BSA and ACN in dH 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 2 O than in buffer solutions

Characterizing the binding interaction of fungicide boscalid with bovine serum albumin (BSA): A spectroscopic study in combination with molecular docking approach.

Science.gov (United States)

Lou, Yan-Yue; Zhou, Kai-Li; Shi, Jie-Hua; Pan, Dong-Qi

2017-08-01

Boscalid, a carboxamide fungicide, is used in the treatment of grey mould and powdery mildew, widely applied to a variety of crops and fruits such as rice, wheat, grapes and pears. It will become a potential risk for health due to its widely application and residue in crops and fruits. In this study, the binding interaction between boscalid and bovine serum albumin (BSA) was characterized using steady-state fluorescence spectroscopy, ultraviolet spectroscopy (UV), synchronous fluorescence spectroscopy, 3D fluorescence spectroscopy, Fourier transform infrared spectroscopy (FT-IR) and molecular docking to ascertain the store, transport and distribution of boscalid in vivo. The experimental results indicated that the fluorescence of BSA was quenched due to the forming the static boscalid-BSA complex with the binding constant of 4.57×10 3 M -1 at 298 K and boscalid bound on the subdomain III A (site II) of BSA through van der Waals force and hydrogen bonding interaction. The binding process of boscalid with BSA was spontaneous and enthalpy-driven process based on ΔG 0 T|ΔS 0 | over the studied temperature range. Meanwhile, the obvious change in the conformation of boscalid was observed while the slight change in the conformation of BSA when binding boscalid to the BSA, implying that the flexibility of boscalid contributes to increasing the stability of the boscalid-BSA complex. Copyright © 2017 Elsevier B.V. All rights reserved.

Resveratrol-loaded glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles: Preparation, characterization, and targeting effect on liver tumors.

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Wu, Mingfang; Lian, Bolin; Deng, Yiping; Feng, Ziqi; Zhong, Chen; Wu, Weiwei; Huang, Yannian; Wang, Lingling; Zu, Chang; Zhao, Xiuhua

2017-08-01

In this study, glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles were prepared to establish a tumor targeting nano-sized drug delivery system. Glycyrrhizic acid was coupled to human serum albumin, and resveratrol was encapsulated in glycyrrhizic acid-conjugated human serum albumin by high-pressure homogenization emulsification. The average particle size of sample nanoparticles prepared under the optimal conditions was 108.1 ± 5.3 nm with a polydispersity index (PDI) of 0.001, and the amount of glycyrrhizic acid coupled with human serum albumin was 112.56 µg/mg. The drug encapsulation efficiency and drug loading efficiency were 83.6 and 11.5%, respectively. The glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles were characterized through laser light scattering, scanning electron microscopy, Fourier-transform infrared spectroscopy, X-ray diffraction, differential scanning calorimetry, thermogravimetric analyses, and gas chromatography. The characterization results showed that resveratrol in glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles existed in amorphous state and the residual amounts of chloroform and methanol in nanoparticles were separately less than the international conference on harmonization (ICH) limit. The in vitro drug-release study showed that the nanoparticles released the drug slowly and continuously. The inhibitory rate of glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles was measured using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2 H-tetrazolium bromide method. The IC50 values of glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles and resveratrol were 62.5 and 95.5 µg/ml, respectively. The target ability of glycyrrhizic acid-conjugated human serum albumin nanoparticles wrapping resveratrol nanoparticles

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 cont...

Inhibition effects of protein-conjugated amorphous zinc sulfide nanoparticles on tumor cells growth

International Nuclear Information System (INIS)

Cao Ying; Wang Huajie; Cao Cui; Sun Yuanyuan; Yang Lin; Wang Baoqing; Zhou Jianguo

2011-01-01

In this article, a facile and environmentally friendly method was applied to fabricate BSA-conjugated amorphous zinc sulfide (ZnS) nanoparticles using bovine serum albumin (BSA) as the matrix. Transmission electron microscopy analysis indicated that the stable and well-dispersed nanoparticles with the diameter of 15.9 ± 2.1 nm were successfully prepared. The energy dispersive X-ray, X-ray powder diffraction, Fourier transform infrared spectrograph, high resolution transmission electron microscope, and selected area electron diffraction measurements showed that the obtained nanoparticles had the amorphous structure and the coordination occurred between zinc sulfide surfaces and BSA in the nanoparticles. In addition, the inhibition effects of BSA-conjugated amorphous zinc sulfide nanoparticles on tumor cells growth were described in detail by cell viability analysis, optical and electron microscopy methods. The results showed that BSA-conjugated amorphous zinc sulfide nanoparticles could inhibit the metabolism and proliferation of human hepatocellular carcinoma cells, and the inhibition was dose dependent. The half maximal inhibitory concentration (IC50) was 0.36 mg/mL. Overall, this study suggested that BSA-conjugated amorphous zinc sulfide nanoparticles had the application potential as cytostatic agents and BSA in the nanoparticles could provide the modifiable site for the nanoparticles to improve their bioactivity or to endow them with the target function.

Albumin nanoparticles with synergistic antitumor efficacy against metastatic lung cancers.

Science.gov (United States)

Kim, Bomi; Seo, Bohyung; Park, Sanghyun; Lee, Changkyu; Kim, Jong Oh; Oh, Kyung Taek; Lee, Eun Seong; Choi, Han-Gon; Youn, Yu Seok

2017-10-01

Albumin nanoparticles are well-known as effective drug carriers used to deliver hydrophobic chemotherapeutic agents. Albumin nanoparticles encapsulating curcumin and doxorubicin were fabricated using slightly modified nanoparticle albumin-bound (nab™) technology, and the synergistic effects of these two drugs were examined. Albumin nanoparticles encapsulating curcumin, doxorubicin, and both curcumin and doxorubicin were prepared using a high pressure homogenizer. The sizes of albumin nanoparticles were ∼130nm, which was considered to be suitable for the EPR (enhanced permeability and retention) effect. Albumin nanoparticles gradually released drugs over a period of 24h without burst effect. To confirm the synergistic effect of two drugs, in vitro cytotoxicity assay was performed using B16F10 melanoma cells. The cytotoxic effect on B16F10 melanoma cells was highest when co-treated with both curcumin and doxorubicin compared to single treatment of either curcumin and doxorubicin. The combined index calculated by medium-effect equation was 0.6069, indicating a synergistic effect. Results of confocal laser scanning microscopy and fluorescence-activated cell sorting corresponded to results from an in vitro cytotoxicity assay, indicating synergistic cytotoxicity induced by both drugs. A C57BL/6 mouse model induced by B16F10 lung metastasis was used to study in vivo therapeutic effects. When curcumin and doxorubicin were simultaneously treated, the metastatic melanoma mass in the lungs macroscopically decreased compared to curcumin or doxorubicin alone. Albumin nanoparticles encapsulating two anticancer drugs were shown to have an effective therapeutic result and would be an excellent way to treat resistant lung cancers. Copyright © 2017 Elsevier B.V. All rights reserved.

Spectroscopic analyses on sonocatalytic damage to bovine serum albumin (BSA) induced by ZnO/hydroxylapatite (ZnO/HA) composite under ultrasonic irradiation

Science.gov (United States)

Wang, Zhiqiu; Li, Ying; Wang, Jun; Zou, Mingming; Gao, Jingqun; Kong, Yumei; Li, Kai; Han, Guangxi

ZnO/hydroxylapatite (ZnO/HA) composite with HA molar content of 6.0% was prepared by the method of precipitation and heat-treated at 500 °C for 40 min and was characterized by powder X-ray diffraction (XRD). The sonocatalytic activities of ZnO/HA composite was carried out through the damage of bovine serum albumin (BSA) in aqueous solution. Furthermore, the effects of several factors on the damage of BSA molecules were evaluated by means of UV-vis and fluorescence spectra. Experimental results indicated that the damage degree of BSA aggravated with the increase of ultrasonic irradiation time, irradiation power and ZnO/HA addition amount, but weakened with the increase of solution acidity and ionic strength. In addition, the damage site to BSA was also studied by synchronous fluorescence technology and the damage site was mainly at tryptophan (Trp) residue. This paper provides a valuable reference for driving sonocatalytic method to treat tumor in clinic application.

Paclitaxel Albumin-stabilized Nanoparticle Formulation

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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.

Fe3O4/BSA particles induce osteogenic differentiation of mesenchymal stem cells under static magnetic field.

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Jiang, Pengfei; Zhang, Yixian; Zhu, Chaonan; Zhang, Wenjing; Mao, Zhengwei; Gao, Changyou

2016-12-01

Differentiation of stem cells is influenced by many factors, yet uptake of the magnetic particles with or without magnetic field is rarely tackled. In this study, iron oxide nanoparticles-loaded bovine serum albumin (BSA) (Fe 3 O 4 /BSA) particles were prepared, which showed a spherical morphology with a diameter below 200 nm, negatively charged surface, and tunable magnetic property. The particles could be internalized into bone marrow mesenchymal stem cells (MSCs), and their release from the cells was significantly retarded under external magnetic field, resulting in almost twice intracellular amount of the particles within 21 d compared to that of the magnetic field free control. Uptake of the Fe 3 O 4 /BSA particles enhanced significantly the osteogenic differentiation of MSCs under a static magnetic field, as evidenced by elevated alkaline phosphatase (ALP) activity, calcium deposition, and expressions of collagen type I and osteocalcin at both mRNA and protein levels. Therefore, uptake of the Fe 3 O 4 /BSA particles brings significant influence on the differentiation of MSCs under magnetic field, and thereby should be paid great attention for practical applications. Differentiation of stem cells is influenced by many factors, yet uptake of the magnetic particles with or without magnetic field is rarely tackled. In this study, iron oxide nanoparticles-loaded bovine serum albumin (BSA) (Fe 3 O 4 /BSA) particles with a diameter below 200nm, negatively charged surface, tunable Fe 3 O 4 content and subsequently adjustable magnetic property were prepared. The particles could be internalized into bone marrow mesenchymal stem cells (MSCs), and their release from the cells was significantly retarded under external magnetic field. Uptake of the Fe 3 O 4 /BSA particles enhanced significantly the osteogenic differentiation of MSCs under a constant static magnetic field, while the magnetic particles and external magnetic field alone do not influence significantly the

Curcumin-incorporated albumin nanoparticles and its tumor image

International Nuclear Information System (INIS)

Gong, Guangming; Wu, Rongchun; Pan, Qinqin; Wang, Kaikai; 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. (paper)

Curcumin-incorporated albumin nanoparticles and its tumor image

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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.

Curcumin-incorporated albumin nanoparticles and its tumor image.

Science.gov (United States)

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

2015-01-30

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.

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

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Azade Taheri

2011-01-01

Full Text Available 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∘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 crosslinker showed no significant effect on the size of nanoparticles but free amino groups of nanoparticles were decreased by increasing the crosslinker. The physicochemical interactions between methotrexate and human serum albumin were investigated by differential scanning calorimetry (DSC. Nanoparticles were more cytotoxic on T47D cells compared to free methotrexate. Moreover, methotrexate-human serum albumin nanoparticles decreased the IC50 value of methotrexate on T47D cells in comparison with free methotrexate.

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

International Nuclear Information System (INIS)

Taheri, A.; Atyabi, F.; Nouri, F.S.; Ahadi, F.; Derakhshan, M.A.; Dinarvand, R.; Atyabi, F.; Ghahremani, M.H.; Ostad, S.N.; Dinarvand, R.; Amini, M.; Ghahremani, M.H.; Ostad, S.N.; Mansoori, P.

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, 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.

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)

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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.

1,3-Bis(2-chloroethyl)-1-nitrosourea-loaded bovine serum albumin nanoparticles with dual magnetic resonance-fluorescence imaging for tracking of chemotherapeutic agents.

Science.gov (United States)

Wei, Kuo-Chen; Lin, Feng-Wei; Huang, Chiung-Yin; Ma, Chen-Chi M; Chen, Ju-Yu; Feng, Li-Ying; Yang, Hung-Wei

To date, knowing how to identify the location of chemotherapeutic agents in the human body after injection is still a challenge. Therefore, it is urgent to develop a drug delivery system with molecular imaging tracking ability to accurately understand the distribution, location, and concentration of a drug in living organisms. In this study, we developed bovine serum albumin (BSA)-based nanoparticles (NPs) with dual magnetic resonance (MR) and fluorescence imaging modalities (fluorescein isothiocyanate [FITC]-BSA-Gd/1,3-bis(2-chloroethyl)-1-nitrosourea [BCNU] NPs) to deliver BCNU for inhibition of brain tumor cells (MBR 261-2). These BSA-based NPs are water dispersible, stable, and biocompatible as confirmed by XTT cell viability assay. In vitro phantoms and in vivo MR and fluorescence imaging experiments show that the developed FITC-BSA-Gd/BCNU NPs enable dual MR and fluorescence imaging for monitoring cellular uptake and distribution in tumors. The T1 relaxivity (R1) of FITC-BSA-Gd/BCNU NPs was 3.25 mM(-1) s(-1), which was similar to that of the commercial T1 contrast agent (R1 =3.36 mM(-1) s(-1)). The results indicate that this multifunctional drug delivery system has potential bioimaging tracking of chemotherapeutic agents ability in vitro and in vivo for cancer therapy.

1,3-Bis(2-chloroethyl-1-nitrosourea-loaded bovine serum albumin nanoparticles with dual magnetic resonance–fluorescence imaging for tracking of chemotherapeutic agents

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Wei KC

2016-08-01

Full Text Available Kuo-Chen Wei,1 Feng-Wei Lin,2 Chiung-Yin Huang,1 Chen-Chi M Ma,3 Ju-Yu Chen,1 Li-Ying Feng,1 Hung-Wei Yang2 1Department of Neurosurgery, Chang Gung Memorial Hospital, School of Medicine, Chang Gung University, Taoyuan, 2Institute of Medical Science and Technology, National Sun Yat-sen University, Kaohsiung, 3Department of Chemical Engineering, National Tsing Hua University, Hsinchu, Taiwan, Republic of China Abstract: To date, knowing how to identify the location of chemotherapeutic agents in the human body after injection is still a challenge. Therefore, it is urgent to develop a drug delivery system with molecular imaging tracking ability to accurately understand the distribution, location, and concentration of a drug in living organisms. In this study, we developed bovine serum albumin (BSA-based nanoparticles (NPs with dual magnetic resonance (MR and fluorescence imaging modalities (fluorescein isothiocyanate [FITC]-BSA-Gd/1,3-bis(2-chloroethyl-1-nitrosourea [BCNU] NPs to deliver BCNU for inhibition of brain tumor cells (MBR 261-2. These BSA-based NPs are water dispersible, stable, and biocompatible as confirmed by XTT cell viability assay. In vitro phantoms and in vivo MR and fluorescence imaging experiments show that the developed FITC-BSA-Gd/BCNU NPs enable dual MR and fluorescence imaging for monitoring cellular uptake and distribution in tumors. The T1 relaxivity (R1 of FITC-BSA-Gd/BCNU NPs was 3.25 mM-1 s-1, which was similar to that of the commercial T1 contrast agent (R1 =3.36 mM-1 s-1. The results indicate that this multifunctional drug delivery system has potential bioimaging tracking of chemotherapeutic agents ability in vitro and in vivo for cancer therapy. Keywords: drug tracking, fluorescence imaging, MR imaging, BSA nanoparticles, cancer therapy

[Effect of BSA on random amplified polymorphic DNA (RAPD) in plants].

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Bian, Cai-Miao; Li, Jun-Min; Jin, Ze-Xin; Ge, Ming-Ju

2002-05-01

Using Metasequoia glyptostroboides and Heptacodium miconioides DNA as templates,the effect of bovine serum albumin (BSA) on RAPD in plants was studied. The results showed that suitable concentrations of BSA used in Metasequoia glyptostroboides and Heptacodium miconioides RAPD were different, which were 0.6 microg/microl and 1 microg/microl, respectively. The inhibition of acetylated BSA on the amplification of plant RAPD could be relieved by BSA. BSA could reduce the dosage of Taq DNA polymerase.

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.

Effect of apatite formation of biphasic calcium phosphate ceramic (BCP) on osteoblastogenesis using simulated body fluid (SBF) with or without bovine serum albumin (BSA)

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Huang, Li [Guangxi Key Laboratory of Regenerative Medicine, Guangxi Medical University, Nanning (China); Department of Orthopaedic Trauma and Hand Surgery, The First Affiliated Hospital of Guangxi Medical University, Nanning (China); Zhou, Bo; Wu, Huayu [Department of Cell Biology & Genetics, School of Premedical Sciences, Guangxi Medical University, Nanning (China); Zheng, Li, E-mail: zhengli224@163.com [Guangxi Key Laboratory of Regenerative Medicine, Guangxi Medical University, Nanning (China); The Medical and Scientific Research Center, Guangxi Medical University, Nanning (China); Zhao, Jinmin, E-mail: zhaojinmin@126.com [Guangxi Key Laboratory of Regenerative Medicine, Guangxi Medical University, Nanning (China); Department of Orthopaedic Trauma and Hand Surgery, The First Affiliated Hospital of Guangxi Medical University, Nanning (China); Guangxi Colleges and Universities Key Laboratory of Regenerative Medicine, Guangxi Medical University, Nanning (China)

2017-01-01

Although biphasic calcium phosphate ceramic (BCP) holds promise in therapy of bone defect, surface mineralization prior to implantation may improve the bioactivity to better integrate with the host. Immersion in simulated body fluid (SBF) and bovine serum albumin-simulated body fluid (BSA-SBF) are common methods to form apatite interface layer. This study was intended to investigate the effect of SBF and BSA-SBF treatment on the bioactivity of BCP in vitro. In this study, osteoblasts were grown on BCP with or without treatment of SBF or BSA-SBF, and detected with general observation, scanning electron microscope (SEM), cell proliferation assay, morphology observation, viability assay, alkaline phosphatase (ALP) activity assay, and osteogenic specific gene expression of alkaline phosphatase (ALPL), bone gamma-carboxyglutamate (gla) protein (BGLAP), bone morphogenetic protein 2 (BMP2), bone sialoprotein (BSP), type I collagen (COLI) and runt-related transcription factor 2 (RUNX2) after culture of 2, 5 and 8 days. As the results shown, BCP pre-incubated in SBF and BSA-SBF up-regulated ALP activity and osteogenic related genes and proteins, which testified the positive effect of SBF and BSA-SBF. Especially, BSA-SBF enhanced the cell growth significantly. This study indicated that treatment by BSA-SBF is of importance for BCP before clinical application. - Highlights: • BCP pre-incubated in SBF and BSA-SBF significantly promoted osteogenic differetiation of osteoblasts. • BSA-SBF enhanced the cell growth more significantly than SBF. • SBF may be a little toxic to osteoblasts.

Strong Antibody Responses Induced by Protein Antigens Conjugated onto the Surface of Lecithin-Based Nanoparticles

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Sloat, Brian R.; Sandoval, Michael A.; Hau, Andrew M.; He, Yongqun; Cui, Zhengrong

2009-01-01

An accumulation of research over the years has demonstrated the utility of nanoparticles as antigen carriers with adjuvant activity. Herein we defined the adjuvanticity of a novel lecithin-based nanoparticle engineered from emulsions. The nanoparticles were spheres of around 200 nm. Model protein antigens, bovine serum albumin (BSA) or Bacillus anthracis protective antigen (PA) protein, were covalently conjugated onto the nanoparticles. Mice immunized with the BSA-conjugated nanoparticles developed strong anti-BSA antibody responses comparable to that induced by BSA adjuvanted with incomplete Freund's adjuvant and 6.5-fold stronger than that induced by BSA adsorbed onto aluminum hydroxide. Immunization of mice with the PA-conjugated nanoparticles elicited a quick, strong, and durable anti-PA antibody response that afforded protection of the mice against a lethal dose of anthrax lethal toxin challenge. The potent adjuvanticity of the nanoparticles was likely due to their ability to move the antigens into local draining lymph nodes, to enhance the uptake of the antigens by antigen-presenting cells (APCs), and to activate APCs. This novel nanoparticle system has the potential to serve as a universal protein-based vaccine carrier capable of inducing strong immune responses. PMID:19729045

Encapsulation of Protein-Polysaccharide HIP Complex in Polymeric Nanoparticles

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Ripal Gaudana

2011-01-01

Full Text Available The objective of the present study is to formulate and characterize a nanoparticulate-based formulation of a macromolecule in a hydrophobic ion pairing (HIP complex form. So far, HIP complexation approach has been studied only for proteins with molecular weight of 10–20 kDa. Hence, we have selected bovine serum albumin (BSA having higher molecular weight (66.3 kDa as a model protein and dextran sulphate (DS as a complexing polymer to generate HIP complex. We have prepared and optimized the HIP complex formation process of BSA with DS. Ionic interactions between basic amino acids of BSA with sulphate groups of DS were confirmed by FTIR analysis. Further, nanoparticles were prepared and characterized with respect to size and surface morphology. We observed significant entrapment of BSA in nanoparticles prepared with minimal amounts of PLGA polymer. Finally, results of circular dichroism and intrinsic fluorescence assay have clearly indicated that HIP complexation and method of nanoparticle preparation did not alter the secondary and tertiary structures of BSA.

Sodium alginate-polyvinyl alcohol-bovin serum albumin coated Fe3O4 nanoparticles as anticancer drug delivery vehicle: Doxorubicin loading and in vitro release study and cytotoxicity to HepG2 and L02 cells.

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Prabha, G; Raj, V

2017-10-01

The challenging part of this work was to research the potential aspects of sodium alginate (SA)-polyvinyl alcohol (PVA)-bovin serum albumin (BSA) coated Fe 3 O 4 nanoparticles (Fe 3 O 4 -SA-PVA-BSA) as a drug delivery system for doxorubicin (DOX). The anticancer drug doxorubicin was selected as a model drug which is powerful for numerous cancer treatments. Superparamagnetic Fe 3 O 4 nanoparticles were prepared by co-precipitation method. The mixture solution of Fe 3 O 4 -sodium alginate (SA) - doxorubicin (DOX) was crosslinked with Ca 2+ to form (Fe 3 O 4 -SA-DOX) nanoparticles and addition of PVA and BSA with (Fe 3 O 4 -SA-DOX) nanoparticles was prepared by coating procedure. Doxorubicin drug loaded NPs were prepared by a simple crosslinking method by calcium chloride solution. The prepared polymer coated magnetic nanoparticles (Fe 3 O 4 -SA-PVA-BSA) were characterized by using SEM, AFM, FT-IR, XRD and VSM. The mean sizes of the obtained drug loaded nanoparticles (Fe 3 O 4 -SA-DOX, Fe 3 O 4 -SA-DOX-PVA and Fe 3 O 4 -SA-DOX-PVA-BSA) were between 240±8.3 and 460±8.7nm and zeta potential of the particles also was evaluated using Malvern Zetasizer which ranged between -48.1±2.3 and -22.4±4.1mV. The encapsulation efficiency, was between 36.2±0.01 and 96.45±2.12. Moreover drug loading and drug release properties of the polymer coated magnetic nanoparticles loaded with doxorubicin (Fe 3 O 4 -SA-DOX-PVA-BSA) were also studied. In addition, the cytotoxicity of the created nanoparticles was performed by using MTT assay analysis which showed that DOX loaded nanoparticles (Fe 3 O 4 -SA-DOX-PVA-BSA) were toxic to HepG2 cell lines and non-toxic to L02 cell lines. The in-vitro drug release was studied by using UV-Visible spectrophotometer at acidic environment (pH5.0) and basic environment (pH7.4) as well as at different temperatures (37°C and 42°C). It was found that DOX drug is released much faster in acidic environment (pH5.0) than in the basic environment (pH7

alpha-Glucosidase-albumin conjugates: effect of chronic administration in mice

International Nuclear Information System (INIS)

Allen, T.M.; Murray, L.; Bhardwaj, D.; Poznansky, M.J.

1985-01-01

Enzyme albumin conjugates have been proposed as a means of increasing the efficacy of enzyme use in vivo and decreasing immune response to the enzyme. Particulate drug carriers, however, have a pronounced tendency to localize in the mononuclear phagocyte (reticuloendothelial) system. The authors have examined in mice the effect on phagocytic index, tissue distribution and organ size of continued administration of conjugates of alpha-glucosidase with either homologous or heterologous albumin. Mice received 10 X 2-mg injections of bovine serum albumin (BSA) or mouse serum albumin (MSA), either free, polymerized or conjugated with alpha-glucosidase. Experiments involving BSA had to be terminated before the end of the experiment because of anaphylaxis, but these reactions were less severe to the polymerized albumin than to free albumin. Free BSA, BSA polymer and BSA-enzyme conjugates all caused a decrease in phagocytic index after six injections. Mice receiving MSA showed no evidence of anaphylaxis, but mice receiving six or more injections of free MSA, MSA polymer or MSA-enzyme conjugate had significantly decreased phagocytic indices as compared to controls. Phagocytic indices had returned to normal by 7 days after the final injection. Tissue distribution of 125 I-labeled albumin preparations was determined in either naive or chronically injected mice

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

International Nuclear Information System (INIS)

Pan Bifeng; Gao Feng; Ao Limei

2005-01-01

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

Effect of cationic grafted copolymer structure on the encapsulation of bovine serum albumin

International Nuclear Information System (INIS)

Flynn, Nicholas; Topal, Ç. Özge; Hikkaduwa Koralege, Rangika S.; Hartson, Steve; Ranjan, Ashish; Liu, Jing; Pope, Carey; Ramsey, Joshua D.

2016-01-01

The aim of the present study was to evaluate a library of poly-L-lysine (PLL)-graft (g)-polyethylene glycol (PEG) copolymers for the ability to encapsulate effectively a model protein, bovine serum albumin (BSA), and to characterize the stability and protein function of the resulting nanoparticle. A library of nine grafted copolymers was produced by varying PLL molecular weight and PEG grafting ratio. Electrostatic self-assembly of the protein and the grafted copolymer drove encapsulation. The formation of protein/polymer nanoparticles with a core/shell structure was confirmed using PAGE, dynamic light scattering, and electron microscopy. Encapsulation of the BSA into nanoparticles was strongly dependent on the copolymer-to-protein mass ratio, PEG grafting ratio, and PLL molecular weight. A copolymer-to-protein mass ratio of 7:1 and higher was generally required for high levels of encapsulation, and under these conditions, no loss of protein activity was observed. Copolymer characteristics also influenced nanoparticle resistance to polyanions and protease degradation. The results indicate that a copolymer of 15–30 kDa PLL, with a PEG grafting ratio of 10:1, is most promising for protein delivery. - Highlights: • A 4–70 kDa range of PLL-g-PEG copolymers was able to encapsulate BSA into NPs. • Encapsulation of BSA by PLL-g-PEG not only retained but increased esterolytic activity. • NPs were stable against protease degradation and polyanion dissociation.

Effect of cationic grafted copolymer structure on the encapsulation of bovine serum albumin

Energy Technology Data Exchange (ETDEWEB)

Flynn, Nicholas [School of Chemical Engineering, Oklahoma State University, Stillwater, OK 74078 (United States); Topal, Ç. Özge [School of Mechanical and Aerospace Engineering, Oklahoma State University, Stillwater, OK 74078 (United States); Hikkaduwa Koralege, Rangika S. [School of Chemical Engineering, Oklahoma State University, Stillwater, OK 74078 (United States); Hartson, Steve [Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078 (United States); Ranjan, Ashish; Liu, Jing; Pope, Carey [Department of Physiological Sciences, Oklahoma State University, Stillwater, OK 74078 (United States); Ramsey, Joshua D., E-mail: josh.ramsey@okstate.edu [School of Chemical Engineering, Oklahoma State University, Stillwater, OK 74078 (United States)

2016-05-01

The aim of the present study was to evaluate a library of poly-L-lysine (PLL)-graft (g)-polyethylene glycol (PEG) copolymers for the ability to encapsulate effectively a model protein, bovine serum albumin (BSA), and to characterize the stability and protein function of the resulting nanoparticle. A library of nine grafted copolymers was produced by varying PLL molecular weight and PEG grafting ratio. Electrostatic self-assembly of the protein and the grafted copolymer drove encapsulation. The formation of protein/polymer nanoparticles with a core/shell structure was confirmed using PAGE, dynamic light scattering, and electron microscopy. Encapsulation of the BSA into nanoparticles was strongly dependent on the copolymer-to-protein mass ratio, PEG grafting ratio, and PLL molecular weight. A copolymer-to-protein mass ratio of 7:1 and higher was generally required for high levels of encapsulation, and under these conditions, no loss of protein activity was observed. Copolymer characteristics also influenced nanoparticle resistance to polyanions and protease degradation. The results indicate that a copolymer of 15–30 kDa PLL, with a PEG grafting ratio of 10:1, is most promising for protein delivery. - Highlights: • A 4–70 kDa range of PLL-g-PEG copolymers was able to encapsulate BSA into NPs. • Encapsulation of BSA by PLL-g-PEG not only retained but increased esterolytic activity. • NPs were stable against protease degradation and polyanion dissociation.

Genotoxicity of Superparamagnetic Iron Oxide Nanoparticles in Granulosa Cells

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Marina Pöttler

2015-11-01

Full Text Available Nanoparticles that are aimed at targeting cancer cells, but sparing healthy tissue provide an attractive platform of implementation for hyperthermia or as carriers of chemotherapeutics. According to the literature, diverse effects of nanoparticles relating to mammalian reproductive tissue are described. To address the impact of nanoparticles on cyto- and genotoxicity concerning the reproductive system, we examined the effect of superparamagnetic iron oxide nanoparticles (SPIONs on granulosa cells, which are very important for ovarian function and female fertility. Human granulosa cells (HLG-5 were treated with SPIONs, either coated with lauric acid (SEONLA only, or additionally with a protein corona of bovine serum albumin (BSA; SEONLA-BSA, or with dextran (SEONDEX. Both micronuclei testing and the detection of γH2A.X revealed no genotoxic effects of SEONLA-BSA, SEONDEX or SEONLA. Thus, it was demonstrated that different coatings of SPIONs improve biocompatibility, especially in terms of genotoxicity towards cells of the reproductive system.

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. Copyright © 2016 Elsevier B.V. All rights reserved.

Rapid detection of Cu(2+) by a paper-based microfluidic device coated with bovine serum albumin (BSA)-Au nanoclusters.

Science.gov (United States)

Fang, Xueen; Zhao, Qianqian; Cao, Hongmei; Liu, Juan; Guan, Ming; Kong, Jilie

2015-11-21

In this work, bovine serum albumin (BSA)-Au nanoclusters were used to coat a paper-based microfluidic device. This device acted as a Cu(2+) biosensor that showed fluorescence quenching on detection of copper ions. The detection limit of this sensor could be adjusted by altering the water absorbing capacity of the device. Qualitative and semi-quantitative results could be obtained visually without the aid of any advanced instruments. This sensor could test Cu(2+) rapidly with high specificity and sensitivity, which would be useful for point-of-care testing (POCT).

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

Fluorescent copper(II complexes: The electron transfer mechanism, interaction with bovine serum albumin (BSA and antibacterial activity

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Madhumita Hazra

2017-01-01

Full Text Available Dinuclear copper(II complexes with formula [Cu2(L2(N32] (1 and [Cu2(L2(NCS2] (2 HL = (1-[(3-methyl-pyridine-2-ylimino-methyl]-naphthalen-2-ol were synthesized by controlling the molar ratio of Cu(OAC2·6H2O, HL, sodium azide (1 and ammonium thiocyanate (2. The end on bridges appear exclusively in azide and thiocyanate to copper complexes. The electron transfer mechanism of copper(II complexes is examined by cyclic voltammetry indicating copper(II complexes are Cu(II/Cu(I couple. The interactions of copper(II complexes towards bovine serum albumin (BSA were examined with the help of absorption and fluorescence spectroscopic tools. We report a superficial solution-based route for the synthesis of micro crystals of copper complexes with BSA. The antibacterial activity of the Schiff base and its copper complexes were investigated by the agar disc diffusion method against some species of pathogenic bacteria (Escherichia coli, Vibrio cholerae, Streptococcus pneumonia and Bacillus cereus. It has been observed that the antibacterial activity of all complexes is higher than the ligand.

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

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....... In both cases we obtained an estimate for the turnover number (TON) of the enzyme reaction....

Human serum albumin mediated self-assembly of gold nanoparticles into hollow spheres

Energy Technology Data Exchange (ETDEWEB)

Nayak, Nimai C [Singapore-MIT Alliance, Manufacturing Systems and Technology Programme, Nanyang Technological University, 65 Nanyang Drive, 637460 (Singapore); Shin, Kwanwoo [Interdisciplinary Program of Integrated Biotechnology, Sogang University, Shinsoo-dong, Mapo-gu, Seoul 121-742 (Korea, Republic of)], E-mail: ncnayak@gmail.com

2008-07-02

The assembly of nanoparticles in topologically predefined superstructures is an important area in nanoscale architecture. In this paper, we report an unusual aggregation phenomenon involving L-lysine capped gold nanoparticles and human serum albumin into hollow nanospheres. The electrostatic interaction between positively charged L-lysine capped gold nanoparticles and negatively charged human serum albumin at physiological pH led to the assembly of the gold nanoparticles into hollow spheres. The phenomenon can be explained by the dry hole opening mechanism.

Human serum albumin mediated self-assembly of gold nanoparticles into hollow spheres

International Nuclear Information System (INIS)

Nayak, Nimai C; Shin, Kwanwoo

2008-01-01

The assembly of nanoparticles in topologically predefined superstructures is an important area in nanoscale architecture. In this paper, we report an unusual aggregation phenomenon involving L-lysine capped gold nanoparticles and human serum albumin into hollow nanospheres. The electrostatic interaction between positively charged L-lysine capped gold nanoparticles and negatively charged human serum albumin at physiological pH led to the assembly of the gold nanoparticles into hollow spheres. The phenomenon can be explained by the dry hole opening mechanism

PENGARUH PENGGANTIAN BOVINE SERUM ALBUMIN (BSA DENGAN PUTIH TELUR DALAM PENGENCER DASAR Cep-2 TERHADAP KUALITAS SEMEN KAMBING BOER PADA SIMPAN DINGIN

Directory of Open Access Journals (Sweden)

Ayu Sulvi Istanty

2017-06-01

Full Text Available The purpose of this research wasinvestigated the substitution effect of Bovine Serum Albumin (BSA with albumen on CEP-2 diluent to semen quality of Boer goat that was stored at 3-50C. Research was conducted at Reproduction Laboratory and Field Laboratory SumberSekarDau Animal Husbandry Faculty of Brawijaya University from December 2016until January 2017. The materials used for this research were fresh semen from 3,5-4,5 years old Boer goat which was collected with artificial vagina. Semen diluent was divided into two groups, those were P0 (90% CEP-2 + 10% Egg Yolk and P1 (90% CEP-2 (without BSA + 0,4% albumen + 10% Egg Yolk. Data of the research were analyzed using paired design t test. The result showed that after eight days of chilled preservation, the sperm motility of P0 was not significantly different with P1 (P>0,05. The average percentage of motility during eight days preservation P0 was higher than P1. The viability between P0 and P1 showed highly significantly difference (P<0,01. The average percentage of viability during eight days preservation P0 was higher than P1. The abnormality between P0 and P1 showed highly significant difference (P<0,01. The average percentage of abnormality between eight dayspreservation P1 was higher than P0. Total motile sperms count after seven days chilled preservation was not significantly different with hope value 40 million motile sperm/ml. The conclusion of this research was the substitution of BSA with albumen could maintain Boer goat semen quality.   Keywords : CEP-2, Bovine SerumAlbumin, Semen, Cryoprotectant

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)

Fluorescence resonance energy transfer between ZnSe ZnS quantum dots and bovine serum albumin in bioaffinity assays of anticancer drugs

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Shu, Chang; Ding, Li; Zhong, Wenying

2014-10-01

In the current work, using ZnSe ZnS quantum dots (QDs) as representative nanoparticles, the affinities of seven anticancer drugs for bovine serum albumin (BSA) were studied using fluorescence resonance energy transfer (FRET). The FRET efficiency of BSA-QD conjugates can reach as high as 24.87% by electrostatic interaction. The higher binding constant (3.63 × 107 L mol-1) and number of binding sites (1.75) between ZnSe ZnS QDs and BSA demonstrated that the QDs could easily associate to plasma proteins and enhance the transport efficacy of drugs. The magnitude of binding constants (103-106 L mol-1), in the presence of QDs, was between drugs-BSA and drugs-QDs in agreement with common affinities of drugs for serum albumins (104-106 L mol-1) in vivo. ZnSe ZnS QDs significantly increased the affinities for BSA of Vorinostat (SAHA), Docetaxel (DOC), Carmustine (BCNU), Doxorubicin (Dox) and 10-Hydroxycamptothecin (HCPT). However, they slightly reduced the affinities of Vincristine (VCR) and Methotrexate (MTX) for BSA. The recent work will not only provide useful information for appropriately understanding the binding affinity and binding mechanism at the molecular level, but also illustrate the ZnSe ZnS QDs are perfect candidates for nanoscal drug delivery system (DDS).

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

International Nuclear Information System (INIS)

Kumaran, R.; Ramamurthy, P.

2014-01-01

Addition. of amides containing a H-CO(NH 2 ) or CH 3 -CO(NH 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 3 ) 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 2 )), whereas a shift in the emission maximum only towards the red region results on the addition of acetamide (CH 3 -CONH 2 ). Steady state emission spectral studies reveal that amides that possess a free NH 2 and N(CH 3 ) 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 DMF 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: • The manuscript deals with the absorption, emission and fluorescence lifetime studies of Bovine Serum Albumin with amides in aqueous medium. • Fluorescence is correlated to the presence of fluorescing amino acid, tryptophan located in a heterogeneous environment. • This article provides an insight about the fluorescence spectral characteristics of a protein

Bisphosphonate-coated BSA nanoparticles lack bone targeting after systemic administration.

Science.gov (United States)

Wang, Guilin; Kucharski, Cezary; Lin, Xiaoyue; Uludağ, Hasan

2010-09-01

A polymeric conjugate of polyethyleneimine-graft-poly(ethylene glycol) and 2-(3-mercaptopropylsulfanyl)-ethyl-1,1-bisphosphonic acid (PEI-PEG-thiolBP) was prepared and used for surface coating of bovine serum albumin (BSA) nanoparticles (NPs) designed for bone-specific delivery of bone morphogenetic protein-2 (BMP-2). The NP coating was achieved with a dialysis and an evaporation method, and the obtained NPs were characterized by particle size, zeta-potential, morphology, and cytotoxicity in vitro. The particle size and surface charge of the NPs could be effectively tuned by the PEG and thiolBP substitution ratios of the conjugate, the coating method, and the polymer concentration used for coating. The PEG modification on PEI reduced the toxicity of PEI and the coated NPs, based on in vitro assessment with human C2C12 cells and rat bone marrow stromal cells. On the basis of an alkaline phosphatase (ALP) induction assay, the NP-encapsulated BMP-2 displayed full retention of its bioactivity, except for BMP-2 in PEI-coated NPs. By encapsulating (125)I-labeled BMP-2, the polymer-coated NPs were assessed for hydroxyapatite (HA) affinity; all NP-encapsulated BMP-2 showed significant affinity to HA as compared with free BMP-2 in vitro, and the PEI-PEG-thiolBP coated NPs improved the in vivo retention of BMP-2 compared with uncoated NPs. However, the biodistribution of NPs after intravenous injection in a rat model indicated no beneficial effects of thiolBP-coated NPs for bone targeting. Our results suggested that the BP-conjugated NPs are useful for localized delivery of BMP-2 in bone repair and regeneration, but they are not effective for bone targeting after intravenous administration.

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.

Interactions of serum albumins with antitumor agent benzo [a] phenazine-a spectroscopic study

International Nuclear Information System (INIS)

Sivakumar, Radhakrishnan; Naveenraj, Selvaraj; Anandan, Sambandam

2011-01-01

We present an investigation on the site specific interaction of antitumor agent benzo [a] phenazine (BAP) with serum albumins (HSA and BSA) and related photo-physical properties using absorption, emission and lifetime measurements. The absorption and emission measurements reveal that the binding of biomolecule benzo [a] phenazine took place near tryptophan moiety present in sub-domain IIA in serum albumins (HSA and BSA). In the selective excitation of benzo [a] phenazine at 365 nm, it was observed that the ground state of serum albumin quenches the excited benzo [a] phenazine through charge transfer exciplexation. The fluorescence decay analysis of serum albumins in the presence of benzo [a] phenazine shows decrease in lifetime, which confirms that photo-induced electron transfer takes place from serum albumins (HSA and BSA) to BAP. Also a suitable mechanism was proposed for the observed photo-induced electron transfer processes. Binding average distance (r) between the donor (serum albumins) and acceptor (benzo [a] phenazine) calculated using FRET theory confirmed their high probability of binding interaction. - Graphical Abstract: Highlights: → Benzo [a] phenazine (BAP) specifically bounds with tryptophan present in HSA and BSA. → Ground state of serum albumin quenches the excited BAP at 365 nm. → Lifetime of serum albumins decreases in the presence of BAP. → Photo-induced electron transfer from HSA and BSA to BAP takes place.

Zinc-decorated silica-coated magnetic nanoparticles for protein binding and controlled release.

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Bele, Marjan; Hribar, Gorazd; Campelj, Stanislav; Makovec, Darko; Gaberc-Porekar, Vladka; Zorko, Milena; Gaberscek, Miran; Jamnik, Janko; Venturini, Peter

2008-05-01

The aim of this study was to be able to reversibly bind histidine-rich proteins to the surface of maghemite magnetic nanoparticles via coordinative bonding using Zn ions as the anchoring points. We showed that in order to adsorb Zn ions on the maghemite, the surface of the latter needs to be modified. As silica is known to strongly adsorb zinc ions, we chose to modify the maghemite nanoparticles with a nanometre-thick silica layer. This layer appeared to be thin enough for the maghemite nanoparticles to preserve their superparamagnetic nature. As a model the histidine-rich protein bovine serum albumin (BSA) was used. The release of the BSA bound to Zn-decorated silica-coated maghemite nanoparticles was analysed using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). We demonstrated that the bonding of the BSA to such modified magnetic nanoparticles is highly reversible and can be controlled by an appropriate change of the external conditions, such as a pH decrease or the presence/supply of other chelating compounds.

Molecular Structure-Affinity Relationship of Flavonoids in Lotus Leaf (Nelumbo nucifera Gaertn.) on Binding to Human Serum Albumin and Bovine Serum Albumin by Spectroscopic Method.

Science.gov (United States)

Tang, Xiaosheng; Tang, Ping; Liu, Liangliang

2017-06-23

Lotus leaf has gained growing popularity as an ingredient in herbal formulations due to its various activities. As main functional components of lotus leaf, the difference in structure of flavonoids affected their binding properties and activities. In this paper, the existence of 11 flavonoids in lotus leaf extract was confirmed by High Performance Liquid Chromatography (HPLC) analysis and 11 flavonoids showed various contents in lotus leaf. The interactions between lotus leaf extract and two kinds of serum albumins (human serum albumin (HSA) and bovine serum albumin (BSA)) were investigated by spectroscopic methods. Based on the fluorescence quenching, the interactions between these flavonoids and serum albumins were further checked in detail. The relationship between the molecular properties of flavonoids and their affinities for serum albumins were analyzed and compared. The hydroxylation on 3 and 3' position increased the affinities for serum albumins. Moreover, both of the methylation on 3' position of quercetin and the C₂=C₃ double bond of apigenin and quercetin decreased the affinities for HSA and BSA. The glycosylation lowered the affinities for HSA and BSA depending on the type of sugar moiety. It revealed that the hydrogen bond force played an important role in binding flavonoids to HSA and BSA.

Study on radiation grafting of NASI on sephadex and conjugation of the copolymer with BSA

International Nuclear Information System (INIS)

Yi Min; Li Jun; Wei Jinshan; Ha Hongfei

1997-01-01

N-acryloxysuccinimide (NASI) with a function ester group is grafted on Sephadex G75 and Sephadex G50 separately by radiation technology. The radiation grafting conditions including absorbed dose, dose rate, monomer concentration in solvent are investigated. The conjugation reactions between the grafted copolymers Sephadex G75-NASI, and bovine serum albumin (BSA) or Sephadex G50-NASI and bovine serum albumin (BSA) are followed. The experiment results show that the conjugate of Sephadex G75-NASI with larger holes and BSA (M r = 6.6 x 10 4 ) is obtained successfully, however, the Sephadex G50 with small holes can be only conjugated with neutral red (M r = 2.58 x 10 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

International Nuclear Information System (INIS)

Kumaran, Rajendran; Vanjinathan, Mahalingam; Ramamurthy, Perumal

2015-01-01

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 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 a

BSA-stabilized Pt nanozyme for peroxidase mimetics and its application on colorimetric detection of mercury(II) ions.

Science.gov (United States)

Li, Wei; Chen, Bin; Zhang, Haixiang; Sun, Yanhua; Wang, Jun; Zhang, Jinli; Fu, Yan

2015-04-15

Bovine serum albumin (BSA) is chosen as the nucleation templates to synthesize Pt-based peroxidase nanomimetics with the average diameter of 2.0nm. The efficient Pt nanozymes consist of 57% Pt(0) and 43% Pt(2+), which possess highly peroxidase-like activity with the Km values of 0.119mM and 41.8mM toward 3,3',5,5'-tetramethylbenzidine (TMB) and hydrogen peroxide (H2O2), respectively. Interestingly, Hg(2+) is able to down-regulate the enzymatic activity of Pt nanoparticles, mainly through the interactions between Hg(2+) and Pt(0). It is the first report to explore a colorimetric Hg(2+) sensing system on the basis of peroxidase mimicking activities of Pt nanoparticles. One of our most intriguing results is that BSA-stabilized Pt nanozymes demonstrate the ability to sense Hg(2+) ions in aqueous solution without significant interference from other metal ions. The Hg(2+) detection limit of 7.2nM is achieved with a linear response range of 0-120nM, and the developed sensing system is potentially applicable for quantitative determination of Hg(2+) in drinking water. Copyright © 2014 Elsevier B.V. All rights reserved.

Studies on the antimicrobial properties of colloidal silver nanoparticles stabilized by bovine serum albumin.

Science.gov (United States)

Mathew, Thomas V; Kuriakose, Sunny

2013-01-01

Colloidal silver nanoparticles were synthesised using sol-gel method and these nanoparticles were stabilised by encapsulated into the scaffolds of bovine serum albumin. Silver nanoparticles and encapsulated products were characterised by FTIR, NMR, XRD, TG, SEM and TEM analyses. Silver nanoparticle encapsulated bovine serum albumin showed highly potent antibacterial activity towards the bacterial strains such as Staphylococcus aureus, Serratia marcescens, Pseudomonas aeruginosa, Escherichia coli and Klebsiella pneumoniae. Copyright © 2012 Elsevier B.V. All rights reserved.

BSA-coated nanoparticles for improved SERS-based intracellular pH sensing.

Science.gov (United States)

Zheng, Xiao-Shan; Hu, Pei; Cui, Yan; Zong, Cheng; Feng, Jia-Min; Wang, Xin; Ren, Bin

2014-12-16

Local microenvironment pH sensing is one of the key parameters for the understanding of many biological processes. As a noninvasive and high sensitive technique, surface-enhanced Raman spectroscopy (SERS) has attracted considerable interest in the detection of the local pH of live cells. We herein develop a facile way to prepare Au-(4-MPy)-BSA (AMB) pH nanosensor. The 4-MPy (4-mercaptopyridine) was used as the pH sensing molecule. The modification of the nanoparticles with BSA not only provides a high sensitive response to pH changes ranging from pH 4.0 to 9.0 but also exhibits a high sensitivity and good biocompatibility, stability, and reliability in various solutions (including the solutions of high ionic strength or with complex composition such as the cell culture medium), both in the aggregation state or after long-term storage. The AMB pH nanosensor shows great advantages for reliable intracellular pH analysis and has been successfully used to monitor the pH distribution of live cells and can address the grand challenges in SERS-based pH sensing for practical biological applications.

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

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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.

Protein coated gold nanoparticles as template for the directed synthesis of highly fluorescent gold nanoclusters

Science.gov (United States)

Zhang, Lingyan; Han, Fei

2018-04-01

Bovine serum albumin (BSA) modified gold nanoparticles (AuNPs) was selected as template for the synthesis of AuNPs@gold nanoclusters (AuNCs) core/shell nanoparticles, in which BSA not only acted as dual functions agent for both anchoring and reducing Au3+ ions, but also was employed as a bridge between the AuNPs and AuNCs. Optical properties of AuNPs@AuNCs core/shell nanoparticles were studied using UV-visible and fluorescence spectroscopy. The prepared AuNPs@AuNCs core/shell nanoparticles exhibited sphere size uniformity with improved monodispersity, excellent fluorescence and fluorescent stability. Compared with AuNCs, AuNPs@AuNCs core/shell nanoparticles possessed large size and strong fluorescence intensity due to the effect of AuNPs as core. Moreover, the mechanism of the AuNPs induced fluorescence changes of the core/shell nanoparticles was first explored.

Sonochemical synthesis of (3-aminopropyl)triethoxysilane-modified monodispersed silica nanoparticles for protein immobilization

International Nuclear Information System (INIS)

Shen, Shou-Cang; Ng, Wai Kiong; Chia, Leonard; Dong, Yuan-Cai; Tan, Reginald B.H.

2011-01-01

Graphical abstract: 3-Aminopropyltriethoxysilane modified monodispersed silica nanoparticles were synthesized by rapid sonochemical co-condensation to achieve high capability for protein immobilization. Highlights: → Amino-modified monodispersed silica nanoparticles were synthesized by rapid co-condensation. → Strong positive charge was created by aminopropyl-modification. → Capability for immobilization of negatively charged protein was enhanced. → Electrostatic interaction between proteins and surface contributed to the enhanced adsorption. -- Abstract: 3-Aminopropyltriethoxysilane modified monodispersed silica nanoparticles were synthesized by a rapid sonochemical co-condensation synthesis procedure. The chemical nature of surface organic modifier on the obtained modified silica nanoparticle was characterized by 13 C and 29 Si MAS Nuclear Magnetic Resonance (NMR) spectroscopies, Fourier-transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA)- differential scanning calorimetry (DSC). Due to the strengthened positive surface charge of the silica nanoparticles by the modification with aminopropyl groups, the capability for bovine serum albumin (BSA) adsorption was significantly increased as compared with bare silica nanoparticles. 80 mg/g BSA was adsorbed on modified silica nanoparticles, whereas only 20 mg/g BSA could be loaded on pure silica nanoparticles. The enhanced positive surface charge repelled proteins with net positive charge and the modified silica nanoparticles exhibited negligible adsorption of lysozyme, thus a selective adsorption of proteins could be achieved.

Sonochemical synthesis of (3-aminopropyl)triethoxysilane-modified monodispersed silica nanoparticles for protein immobilization

Energy Technology Data Exchange (ETDEWEB)

Shen, Shou-Cang, E-mail: shen_shoucang@ices.a-star.edu.sg [Institute of Chemical and Engineering Sciences, A-STAR (Agency for Science, Technology and Research), 1 Pesek Road, Jurong Island, Singapore 627833 (Singapore); Ng, Wai Kiong; Chia, Leonard; Dong, Yuan-Cai [Institute of Chemical and Engineering Sciences, A-STAR (Agency for Science, Technology and Research), 1 Pesek Road, Jurong Island, Singapore 627833 (Singapore); Tan, Reginald B.H., E-mail: reginald_tan@ices.a-star.edu.sg [Institute of Chemical and Engineering Sciences, A-STAR (Agency for Science, Technology and Research), 1 Pesek Road, Jurong Island, Singapore 627833 (Singapore); Department of Chemical and Biomolecular Engineering, The National University of Singapore, 4 Engineering Drive 4, Singapore 117576 (Singapore)

2011-10-15

Graphical abstract: 3-Aminopropyltriethoxysilane modified monodispersed silica nanoparticles were synthesized by rapid sonochemical co-condensation to achieve high capability for protein immobilization. Highlights: {yields} Amino-modified monodispersed silica nanoparticles were synthesized by rapid co-condensation. {yields} Strong positive charge was created by aminopropyl-modification. {yields} Capability for immobilization of negatively charged protein was enhanced. {yields} Electrostatic interaction between proteins and surface contributed to the enhanced adsorption. -- Abstract: 3-Aminopropyltriethoxysilane modified monodispersed silica nanoparticles were synthesized by a rapid sonochemical co-condensation synthesis procedure. The chemical nature of surface organic modifier on the obtained modified silica nanoparticle was characterized by {sup 13}C and {sup 29}Si MAS Nuclear Magnetic Resonance (NMR) spectroscopies, Fourier-transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA)- differential scanning calorimetry (DSC). Due to the strengthened positive surface charge of the silica nanoparticles by the modification with aminopropyl groups, the capability for bovine serum albumin (BSA) adsorption was significantly increased as compared with bare silica nanoparticles. 80 mg/g BSA was adsorbed on modified silica nanoparticles, whereas only 20 mg/g BSA could be loaded on pure silica nanoparticles. The enhanced positive surface charge repelled proteins with net positive charge and the modified silica nanoparticles exhibited negligible adsorption of lysozyme, thus a selective adsorption of proteins could be achieved.

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

Interaction of amphiphilic drugs with human and bovine serum albumins.

Science.gov (United States)

Khan, Abbul Bashar; Khan, Javed Masood; Ali, Mohd Sajid; Khan, Rizwan Hasan; Kabir-Ud-Din

2012-11-01

To know the interaction of amphiphilic drugs nortriptyline hydrochloride (NOT) and promazine hydrochloride (PMZ) with serum albumins (i.e., human serum albumin (HSA) and bovine serum albumin (BSA)), techniques of UV-visible, fluorescence, and circular dichroism (CD) spectroscopies are used. The binding affinity is more in case of PMZ with both the serum albumins. The quenching rate constant (k(q)) values suggest a static quenching process for all the drug-serum albumin interactions. The UV-visible results show that the change in protein conformation of PMZ-serum albumin interactions are more prominent as compared to NOT-serum albumin interactions. The CD results also explain the conformational changes in the serum albumins on binding with the drugs. The increment in %α-helical structure is slightly more for drug-BSA complexes as compared to drug-HSA complexes. Copyright © 2012 Elsevier B.V. All rights reserved.

Bovine Serum Albumin binding to CoCrMo nanoparticles and the influence on dissolution

International Nuclear Information System (INIS)

Simoes, T A; Brown, A P; Milne, S J; Brydson, R M D

2015-01-01

CoCrMo alloys exhibit good mechanical properties, excellent biocompatibility and are widely utilised in orthopaedic joint replacements. Metal-on-metal hip implant degradation leads to the release of metal ions and nanoparticles, which persist through the implant's life and could be a possible cause of health complications. This study correlates preferential binding between proteins and metal alloy nanoparticles to the alloy's corrosion behaviour and the release of metal ions. TEM images show the formation of a protein corona in all particles immersed in albumin containing solutions. Only molybdenum release was significant in these tests, suggesting high dissolution of this element when CoCrMo alloy nanoparticles are produced as wear debris in the presence of serum albumin. The same trend was observed during extended exposure of molybdenum reference nanoparticles to albumin. (paper)

Protein-Based Nanoparticle Preparation via Nanoprecipitation Method

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Mohamad Tarhini

2018-03-01

Full Text Available Nanoparticles are nowadays largely investigated in the field of drug delivery. Among nanoparticles, protein-based particles are of paramount importance since they are natural, biodegradable, biocompatible, and nontoxic. There are several methods to prepare proteins containing nanoparticles, but only a few studies have been dedicated to the preparation of protein- based nanoparticles. Then, the aim of this work was to report on the preparation of bovine serum albumin (BSA-based nanoparticles using a well-defined nanoprecipitation process. Special attention has been dedicated to a systematic study in order to understand separately the effect of each operating parameter of the method (such as protein concentration, solvent/non-solvent volume ratio, non-solvent injection rate, ionic strength of the buffer solution, pH, and cross-linking on the colloidal properties of the obtained nanoparticles. In addition, the mixing processes (batch or drop-wise were also investigated. Using a well-defined formulation, submicron protein-based nanoparticles have been obtained. All prepared particles have been characterized in terms of size, size distribution, morphology, and electrokinetic properties. In addition, the stability of nanoparticles was investigated using Ultraviolet (UV scan and electrophoresis, and the optimal conditions for preparing BSA nanoparticles by the nanoprecipitation method were concluded.

Dissolution, agglomerate morphology, and stability limits of protein-coated silver nanoparticles.

Science.gov (United States)

Martin, Matthew N; Allen, Andrew J; MacCuspie, Robert I; Hackley, Vincent A

2014-09-30

Little is understood regarding the impact that molecular coatings have on nanoparticle dissolution kinetics and agglomerate formation in a dilute nanoparticle dispersion. Dissolution and agglomeration processes compete in removing isolated nanoparticles from the dispersion, making quantitative time-dependent measurements of the mechanisms of nanoparticle loss particularly challenging. In this article, we present in situ ultra-small-angle X-ray scattering (USAXS) results, simultaneously quantifying dissolution, agglomeration, and stability limits of silver nanoparticles (AgNPs) coated with bovine serum albumin (BSA) protein. When the BSA corona is disrupted, we find that the loss of silver from the nanoparticle core is well matched by a second-order kinetic rate reaction, arising from the oxidative dissolution of silver. Dissolution and agglomeration are quantified, and morphological transitions throughout the process are qualified. By probing the BSA-AgNP suspension around its stability limits, we provide insight into the destabilization mechanism by which individual particles rapidly dissolve as a whole rather than undergo slow dissolution from the aqueous interface inward, once the BSA layer is breached. Because USAXS rapidly measures over the entire nanometer to micrometer size range during the dissolution process, many insights are also gained into the stabilization of NPs by protein and its ability to protect the labile metal core from the solution environment by prohibiting the diffusion of reactive species. This approach can be extended to a wide variety of coating molecules and reactive metal nanoparticle systems to carefully survey their stability limits, revealing the likely mechanisms of coating breakdown and ensuing reactions.

Self-Assembled Fluorescent Bovine Serum Albumin Nanoprobes for Ratiometric pH Measurement inside Living Cells.

Science.gov (United States)

Yang, Qiaoyu; Ye, Zhongju; Zhong, Meile; Chen, Bo; Chen, Jian; Zeng, Rongjin; Wei, Lin; Li, Hung-wing; Xiao, Lehui

2016-04-20

In this work, we demonstrated a new ratiometric method for the quantitative analysis of pH inside living cells. The structure of the nanosensor comprises a biofriendly fluorescent bovine serum albumin (BSA) matrix, acting as a pH probe, and pH-insensitive reference dye Alexa 594 enabling ratiometric quantitative pH measurement. The fluorescent BSA matrix was synthesized by cross-linking of the denatured BSA proteins in ethanol with glutaraldehyde. The size of the as-synthesized BSA nanoparticles can be readily manipulated from 30 to 90 nm, which exhibit decent fluorescence at the peak wavelength of 535 nm with a pH response range of 6-8. The potential of this pH sensor for intracellular pH monitoring was demonstrated inside living HeLa cells, whereby a significant change in fluorescence ratio was observed when the pH of the cell was switched from normal to acidic with anticancer drug treatment. The fast response of the nanosensor makes it a very powerful tool in monitoring the processes occurring within the cytosol.

Biological nanoparticles carrying the Hmda-7 gene are effective in inhibiting pancreatic cancer in vitro and in vivo.

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Qingyun Zhu

Full Text Available Pancreatic cancer is one of the most common malignancies of the digestive system, and remains a clinical challenge. This study aimed to assess the effects of bovine serum albumin (BSA nanoparticles carrying the hMDA-7 gene (BSA-NP-hMDA-7 in the treatment of pancreatic cancer.BSA-NP-hMDA-7 was generated by nanotechnology and gene recombination technology. A total of 5 BXPC-3 or PANC-1 pancreatic cancer cell groups were examined, including Control, BSA-NPs, Empty vector, hMDA-7 plasmid, and hMDA-7 BSA-NPs groups, respectively. Proliferation and apoptosis of cultured cells were assessed by the MTT method and flow-cytometry, respectively. In addition, pancreatic cancer models were established with both cell lines in nude mice, and the expression profiles of hMDA-7 and VEGF in cancer tissues were measured by Western blot and immunohistochemistry.BSA-NP-hMDA-7 nanoparticles were successfully generated, and significantly inhibited the proliferation of BXPC-3 and PANC-1 cells; in addition, apoptosis rates were higher in both cell lines after treatment with BSA-NP-hMDA-7 (P<0.05. Nude mouse xenograft studies indicated that treatment with BSA-NP-hMDA-7 nanoparticles resulted in decreased tumor size. Moreover, the hMDA-7 protein was found in tumor tissues after hMDA-7 gene transfection, while BSA-NP-hMDA-7 significantly suppressed VEGF expression in tumor tissues. Similar results were obtained for both BXPC-3 and PANC-1 xenograft models.BSA nanoparticles carrying the hMDA-7 gene effectively transfected BXPC-3 and PANC-1 pancreatic cancer cells, causing reduced cell proliferation and enhanced apoptosis in vitro. In mouse xenografts, BSA-NP-hMDA-7 treatment decreased tumor size and reduced VEGF expression. These findings indicated that BSA-NP-hMDA-7 might exert anticancer effects via VEGF suppression.

Green synthesis of zero-valent Fe-nanoparticles: Catalytic degradation of rhodamine B, interactions with bovine serum albumin and their enhanced antimicrobial activities.

Science.gov (United States)

Khan, Zaheer; Al-Thabaiti, Shaeel Ahmad

2018-03-01

Biomimetic method was used for the synthesis of Fe-nanoparticles (FeNPs). FeCl 3 and Hibiscus sabdariffa, Roselle flower aqueous extract (HBS) were employed in the present studies. The FeNPs have been characterized by using UV-visible spectroscopy, transmission electron microscope (TEM), and energy dispersion X-ray spectroscopy (EDS). The average particles diameter was found to be 18 nm. The as prepared FeNPs were used as a catalyst to the oxidative degradation of rhodamine B (RB) in presence of NaBH 4 . The effects of various quencher on the degradation rates were examined by employing ammonium oxalate (AO), benzoquinone (BQ), isopropyl alcohol (IPA), and potassium iodide (KI). The interactions of FeNPs with bovine serum albumin (BSA) have been determined and discussed. Adsorption of FeNPs into the core of BSA changes the tryptophan environment from hydrophobic to hydrophilic (from folding to partially folded and/or unfolded). Tryptophan residues, indole moieties of BSA were responsible to complex formation with FeNPs in excited states via electrostatic, van der Waals, hydrogen bonding, hydrophobic and hydrophilic interactions with static quenching. The antimicrobial activities of FeNPs have been determined against human pathogens. Hibiscus sabdariffa flower extract shows mild antimicrobial activities against all target pathogenic organisms. FeNPs have potential antimicrobial activity against both bacterial strains and candida fungus even at low concentration, and retains potential application in biomedical industries. Copyright © 2018 Elsevier B.V. All rights reserved.

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

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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

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

Science.gov (United States)

Cohen, Sarit; Margel, Shlomo

2012-08-14

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. 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. 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. 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 nanoparticles, in order to use them for both detection as well as therapy of colon

Spectroscopic analysis of the interaction between tetra-(p-sulfoazophenyl-4-aminosulfonyl-substituted aluminum (III phthalocyanines and serum albumins

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Liqin Zheng

2017-03-01

Full Text Available The binding interaction between tetra-(p-sulfoazophenyl-4-aminosulfonyl-substituted aluminum (III phthalocyanine (AlPc, and two-serum albumins (bovine serum albumin (BSA and human serum albumin (HSA has been investigated. AlPc could quench the intrinsic fluorescence of BSA and HSA through a static quenching process. The primary and secondary binding sites of AlPc on BSA were domain I and III of BSA. The primary binding site of AlPc on HSA was domain I, and the secondary binding sites of AlPc on HSA were found at domains I and II. Our results suggest that AlPc readily interact with BSA and HSA implying that the amphiphilic substituents AlPc may contribute to their transportation in the blood.

The Effect of Albumin on MRP2 and BCRP in the Vesicular Transport Assay.

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Feng Deng

Full Text Available The ABC transporters multidrug resistance associated protein 2 (MRP2 and breast cancer resistance protein (BCRP are of interest in drug development, since they affect the pharmacokinetics of several drugs. Membrane vesicle transport assays are widely used to study interactions with these proteins. Since albumin has been found to affect the kinetics of metabolic enzymes in similar membrane preparations, we investigated whether albumin affects the kinetic parameters of efflux transport. We found that albumin increased the Vmax of 5(6-carboxy-2',7'-dichlorofluorescein (CDCF and estradiol-17-β-D-glucuronide uptake into MRP2 vesicles in the presence of 0.1% bovine serum albumin (BSA by 2 and 1.5-fold, respectively, while BSA increased Lucifer yellow uptake by 30% in BCRP vesicles. Km values increased slightly, but the change was not statistically significant. The effect of BSA on substrate uptake was dependent on the vesicle amount, while increasing BSA concentration did not significantly improve substrate uptake. These results indicate a minor effect of albumin on MRP2 and BCRP, but it should be considered if albumin is added to transporter assays for example as a solubilizer, since the effect may be substrate or transporter specific.

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

International Nuclear Information System (INIS)

Cohen, Sarit; Pellach, Michal; Kam, Yossi; Grinberg, Igor; Corem-Salkmon, Enav; Rubinstein, Abraham; Margel, Shlomo

2013-01-01

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: ► 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.

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

International Nuclear Information System (INIS)

Subia, B; Kundu, S C

2013-01-01

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)

Neutrophil-Mediated Delivery of Therapeutic Nanoparticles across Blood Vessel Barrier for Treatment of Inflammation and Infection.

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Chu, Dafeng; Gao, Jin; Wang, Zhenjia

2015-12-22

Endothelial cells form a monolayer in lumen of blood vessels presenting a great barrier for delivery of therapeutic nanoparticles (NPs) into extravascular tissues where most diseases occur, such as inflammation disorders and infection. Here, we report a strategy for delivering therapeutic NPs across this blood vessel barrier by nanoparticle in situ hitchhiking activated neutrophils. Using intravital microscopy of TNF-α-induced inflammation of mouse cremaster venules and a mouse model of acute lung inflammation, we demonstrated that intravenously (iv) infused NPs made from denatured bovine serum albumin (BSA) were specifically internalized by activated neutrophils, and subsequently, the neutrophils containing NPs migrated across blood vessels into inflammatory tissues. When neutrophils were depleted using anti-Gr-1 in a mouse, the transport of albumin NPs across blood vessel walls was robustly abolished. Furthermore, it was found that albumin nanoparticle internalization did not affect neutrophil mobility and functions. Administration of drug-loaded albumin NPs markedly mitigated the lung inflammation induced by LPS (lipopolysaccharide) or infection by Pseudomonas aeruginosa. These results demonstrate the use of an albumin nanoparticle platform for in situ targeting of activated neutrophils for delivery of therapeutics across the blood vessel barriers into diseased sites. This study demonstrates our ability to hijack neutrophils to deliver nanoparticles to targeted diseased sites.

Exploration of zwitterionic cellulose acetate antifouling ultrafiltration membrane for bovine serum albumin (BSA) separation.

Science.gov (United States)

Liu, Yang; Huang, Haitao; Huo, Pengfei; Gu, Jiyou

2017-06-01

This study focused on the preparation of a new kind of membrane material, zwitterionic cellulose acetate (ZCA), via a three-step procedure consist of oxidization, Schiff base and quaternary amination reaction, and the fabrication of antifouling ZCA ultrafiltration membrane by the non-solvent-induced phase separation method (NIPS). The morphologies, surface chemical structures and compositions of the obtained CA and ZCA membranes were thoroughly characterized by field emission scanning electron microscopy (FE-SEM) with energy dispersive X-ray (EDX) spectroscopy, Fourier transform infrared spectroscopy (FTIR) and X-ray photoelectron spectroscopy (XPS), respectively. Meanwhile, the thermal stability, porosity and average pore size of two investigated membranes were also studied. As a result, the ZCA membrane displayed significantly improved hydrophilicity and water permeability compared with those of the reference CA membrane, despite a slight decrease in the protein rejection ratio. According to the cycle ultrafiltration performance of bovine serum albumin (BSA) solution and protein adsorption experiment, ZCA membrane exhibited better flux recovery property and fouling resistant ability, especially irreversible fouling resistant ability, suggesting superior antifouling performance. This new approach gives polymer-based membrane a long time life and excellent ultrafiltration performance, and seems promising for potential applications in the protein separation. Copyright © 2017 Elsevier Ltd. All rights reserved.

Sucrose/bovine serum albumin mediated biomimetic crystallization

Indian Academy of Sciences (India)

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 ...

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

International Nuclear Information System (INIS)

Rodrigues, Marcilene M.A.; Simioni, Andreza R.; Primo, Fernando L.; Siqueira-Moura, Marigilson P.; Morais, Paulo C.; Tedesco, Antonio C.

2009-01-01

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.

Affinity study on bovine serum albumin's peptides to amphiphilic gold nanoparticles: A test of epitopes and non-epitopes

Science.gov (United States)

Yuan, Ming; Li, Wanrong; Yang, Mingming; Huang, Xiufeng; Bai, Zhijun; Liu, Yushuang; Cai, Weijun; Wang, Yuqin; Zhang, Feng

2017-09-01

It is an inevitable event that nanoparticles (NPs) will encounter proteins/peptides in nano-medicine, so it has been significant to know their interaction mechanism before in vivo applications. Previously, a 105-amino-acid sequence had been reported as the binding site between bovine serum albumin (BSA) and amphiphilic polymer coated gold nanoparticles (AP-AuNPs) along with a mortise-tenon joint hypothesis. This article tested the affinity difference between two epitope peptide sequences such as: LGEYGFQNALIVR (S1), DAFLGSFLYEYSR (S2) and one non-epitope peptide sequence as: FDEHVKLVNELTEF (S3). With the photoluminescent amino acid residues, the fluorescence quenching method based on the nanometal surface energy transfer (NSET) principle was able to study the thermodynamics of the current binding system. The binding constants (Ka) were determined and followed the order as: Ka-S1 > Ka-S2 >> Ka-S3. Moreover, Hill constants indicated that cooperativity only presented in the interactions of AP-AuNP with either S1 or S2, but not for S3. Moreover, gel electrophoresis, surface plasmon resonance, atomic force microscopy and three dimensional fluorescence microscopy were all also used to comprehensively analyse the binding interaction mechanism. These results further provided useful information to better understand the mortise-tenon joint, which might find applications to nanofabrication and biomedicine.

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.

Design and characterization of protein-quercetin bioactive nanoparticles

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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.

Direct comparison of two albumin-based paclitaxel-loaded nanoparticle formulations: is the crosslinked version more advantageous?

Science.gov (United States)

Li, Chunlei; Li, Yanhui; Gao, Yuqing; Wei, Na; Zhao, Xi; Wang, Caixia; Li, Yongfeng; Xiu, Xian; Cui, Jingxia

2014-07-01

Nanoparticles using albumin as particle matrix have entered the mainstream of drug delivery. It was reported that non-crosslinked albumin nanoparticles were unstable in circulation and could deliver drugs into tumor through gp60/SPARC pathway; in contrast, the delivery of drugs with stable nanoparticles was dependent on enhanced permeability and retention effect. Thus, it is questionable which kind of nanoparticles was more advantageous. Two versions of albumin-bound paclitaxel nanoparticles were prepared. In vitro, the non-crosslinked particles could rapidly disintegrate and the crosslinked was stable. The pharmacokinetics of both formulations was different especially at early time and the non-crosslinked particles were cleared rapidly. After non-crosslinked particle treatment paclitaxel had a tendency to accumulate into heart and kidney and following therapy with the crosslinked particles, paclitaxel was liable to be delivered into lung, spleen and liver. The delivery efficiency of paclitaxel into tumor following the non-crosslinked particle treatment was greater than that of the crosslinked (palbumin nanoparticles. Copyright © 2014 Elsevier B.V. All rights reserved.

Studies of quality control of 99mTc-labelled macroaggregated albumin: Pt. 1

International Nuclear Information System (INIS)

Fukuoka, Masamichi; Kobayashi, Tetsu; Tanaka, Akira; Satoh, Takemichi; Kubodera, Akiko

1993-01-01

The aggregative condition of albumin was investigated using bovine serum albumin (BSA) as a model for quality control of 99m Tc-macroaggregated albumin ( 99 Tc-MAA). Uniformalized aggregates were obtained from the oxidized non-mercapt-type of BSA by heating. The size of the aggregates was affected by the pH and the types of buffer solutions used as well as the concentrations of albumin and buffers. The β form structure of the albumin was more stable on heating and this may contribute to its aggregation. Aggregation of oxidized non-mercaptalbumin afforded a portion of smaller sized particles in MAA, this being an inappropriate factor for scintiscanning of lungs. Our results suggest that it is necessary to remove oxidized type albumin from human serum albumin as the starting material, in order to prepare MAA with a uniform and larger particle size. (Author)

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

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.

Characterization of the complex between native and reduced bovine serum albumin with aquacobalamin and evidence of dual tetrapyrrole binding.

Science.gov (United States)

Dereven'kov, Ilia A; Hannibal, Luciana; Makarov, Sergei V; Makarova, Anna S; Molodtsov, Pavel A; Koifman, Oskar I

2018-05-02

Serum albumin binds to a variety of endogenous ligands and drugs. Human serum albumin (HSA) binds to heme via hydrophobic interactions and axial coordination of the iron center by protein residue Tyr161. Human serum albumin binds to another tetrapyrrole, cobalamin (Cbl), but the structural and functional properties of this complex are poorly understood. Herein, we investigate the reaction between aquacobalamin (H 2 OCbl) and bovine serum albumin (BSA, the bovine counterpart of HSA) using Ultraviolet-Visible and fluorescent spectroscopy, and electron paramagnetic resonance. The reaction between H 2 OCbl and BSA led to the formation of a BSA-Cbl(III) complex consistent with N-axial ligation (amino). Prior to the formation of this complex, the reactants participate in an additional binding event that has been examined by fluorescence spectroscopy. Binding of BSA to Cbl(III) reduced complex formation between the bound cobalamin and free cyanide to form cyanocobalamin (CNCbl), suggesting that the β-axial position of the cobalamin may be occupied by an amino acid residue from the protein. Reaction of BSA containing reduced disulfide bonds with H 2 OCbl produces cob(II)alamin and disulfide with intermediate formation of thiolate Cbl(III)-BSA complex and its decomposition. Finally, in vitro studies showed that cobalamin binds to BSA only in the presence of an excess of protein, which is in contrast to heme binding to BSA that involves a 1:1 stoichiometry. In vitro formation of BSA-Cbl(III) complex does not preclude subsequent heme binding, which occurs without displacement of H 2 OCbl bound to BSA. These data suggest that the two tetrapyrroles interact with BSA in different binding pockets.

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

Energy Technology Data Exchange (ETDEWEB)

Guo, Jun; Zhong, Ruibo; Li, Wanrong; Liu, Yushuang; Bai, Zhijun; Yin, Jun; Liu, Jingran; Gong, Pei [Agricultural Nanocenter, School of Life Science, Inner Mongolia Agricultural University, 306 Zhaowuda Road, Hohhot 010018 (China); Zhao, Xinmin, E-mail: zhao.xinmin@hotmail.com [School of Foreign Language, Inner Mongolia Agricultural University, 306 Zhaowuda Road, Hohhot 010018 (China); Zhang, Feng, E-mail: fengzhang1978@hotmail.com [Agricultural Nanocenter, School of Life Science, Inner Mongolia Agricultural University, 306 Zhaowuda Road, Hohhot 010018 (China)

2015-12-30

Graphical abstract: With the non-uniform coating of amphiphilic polymer, the silver nanoparticles (AgNPs) can form protein coronas which can become discrete protein–nanoparticle conjugates when controlling the protein–nanoparticle molar ratios. The protein's conformational changes upon binding NPs was also studied by both circular dichroism and three-dimensional fluorescence spectroscopy. - Highlights: • The amphiphilic polymer coating can not only transfer hydrophobic NPs into water soluble, but also providing a thick shell responsible for the strong physisorption to proteins without significantly changing their spatial conformations. • NP with discrete proteins can be simply obtained by a simple mixing procedure followed by a gel electrophoresis separation, and the resulting conjugates are robust enough to resist common separation techniques like gel electrophoresis. • In combination with the universal amphiphilic polymer coating strategy and the physisorption mediated protein–NP conjugation, proteins like BSA can be effectively conjugated to different materials such as noble metal, semiconductor and magnetic NPs. • In contrast to chemical coupling methods, the physisorption mediated protein–NP conjugation holds facile, robust and reversible advantages, which may find wide applications in nano-biomedicine field. - Abstract: 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 × 10{sup 7} M{sup −1} and the interaction was spontaneously driven by mainly the van der Waals force and

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

Science.gov (United States)

Zhang, Qiulan; Ni, Yongnian; Kokot, Serge

2016-04-07

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.

Surface functionalization of zirconium dioxide nano-adsorbents with 3-aminopropyl triethoxysilane and promoted adsorption activity for bovine serum albumin

International Nuclear Information System (INIS)

Liu, Gen; Wu, Chaochao; Zhang, Xia; Liu, Yufeng; Meng, Hao; Xu, Junli; Han, Yide; Xu, Xinxin; Xu, Yan

2016-01-01

Surface functionalization of zirconium dioxide (ZrO_2) nano-adsorbents was carried out by using 3-aminopropyl triethoxysilane (APTES) as the modifier. The addition amount of APTES was varied to determine the optimum modification extent, and the bulk ZrO_2 microparticles were also modified by APTES for comparison. Some means, such as TEM, XRD, FT-IR, XPS and TG-DSC were used to character these ZrO_2 particles. The results showed that the APTES molecules were chemically immobilized on the surface of ZrO_2 nanoparticles via Zr−O−Si bonds, and the nano-ZrO_2 samples showed larger special surface area. In the adsorption of bovine serum albumin (BSA), nano-ZrO_2 samples exhibited enhanced adsorption activity, and APTES modified nano-ZrO_2 with proper APTES content presented the best adsorption property. Under the same adsorption conditions, the equilibrium adsorption capacity of BSA on APTES-ZrO_2-2 was almost 2.3 times as that on pristine nano-ZrO_2 and 3.0 times as on bulk ZrO_2 microparticles. The increased adsorption capacity of APTES-ZrO_2 nano-adsorbents can be attributed to the chemical interaction between amino and carboxyl groups at APTES-ZrO_2/BSA interface. The pH-dependent experiments showed that the optimum pH value for the adsorption and desorption was 5.0 and 9.0, respectively, which suggested that the adsorption and release of BSA could be controlled simply by adjusting the solution pH condition. - Highlights: • APTES chemically immobilized on ZrO_2 nanoparticles via Zr−O−Si bond. • Enhanced adsorption capacity of BSA was observed on APTES-ZrO_2. • Chemical adsorption character of BSA on APTES-ZrO_2. • Adsorption/release of BSA on APTES-ZrO_2 accomplished by adjusting pH value.

Electrospray ionization deposition of BSA under vacuum conditions

Science.gov (United States)

Hecker, Dominic; Gloess, Daniel; Frach, Peter; Gerlach, Gerald

2015-05-01

Vacuum deposition techniques like thermal evaporation and CVD with their precise layer control and high layer purity often cannot be applied for the deposition of chemical or biological molecules. The molecules are usually decomposed by heat. To overcome this problem, the Electrospray ionization (ESI) process known from mass spectroscopy is employed to transfer molecules into vacuum and to deposit them on a substrate. In this work, a homemade ESI tool was used to deposit BSA (Bovine serum albumin) layers with high deposition rates. Solutions with different concentrations of BSA were prepared using a methanol:water (MeOH:H2O) mixture (1:1) as solvent. The influence of the substrate distance on the deposition rate and on the transmission current was analyzed. Furthermore, the layer thickness distribution and layer adhesion were investigated.

Synthesis and Adsorption Study of BSA Surface Imprinted Polymer on CdS Quantum Dots

Science.gov (United States)

Tang, Ping-ping; Cai, Ji-bao; Su, Qing-de

2010-04-01

A new bovine serum albumin (BSA) surface imprinting method was developed by the incorporation of quantum dots (QDs) into molecularly imprinted polymers (MIP), which can offer shape selectivity. Preparation and adsorption conditions were optimized. Physical appearance of the QDs and QDs-MIP particles was illustrated by scanning electron microscope images. Photoluminescence emission of CdS was quenched when rebinding of the template. The quenching of photoluminescence emissions is presumably due to the fluorescence resonance energy transfer between quantum dots and BSA template molecules. The adsorption is compiled with Langmuir isotherm, and chemical adsorption is the rate-controlling step. The maximum adsorption capacity could reach 226.0 mg/g, which is 142.4 mg/g larger than that of undoped BSA MIP. This study demonstrates the validity of QDs coupled with MIP technology for analyzing BSA.

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

Energy Technology Data Exchange (ETDEWEB)

Kaboudin, B., E-mail: kaboudin@iasbs.ac.ir [Department of Chemistry, Institute for Advanced Studies in Basic Sciences (IASBS), Gava Zang, Zanjan 45137-66731 (Iran, Islamic Republic of); Moradi, K.; Faghihi, M.R.; Mohammadi, F. [Department of Chemistry, Institute for Advanced Studies in Basic Sciences (IASBS), Gava Zang, Zanjan 45137-66731 (Iran, Islamic Republic of)

2013-07-15

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 K{sub A} 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.

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

International Nuclear Information System (INIS)

Kaboudin, B.; Moradi, K.; Faghihi, M.R.; Mohammadi, F.

2013-01-01

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 K A 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

Characterization of the interaction between 3-Oxotabersonine and two serum albumins by using spectroscopic techniques

International Nuclear Information System (INIS)

Wang, Qing; Yan, Jin; He, Jiawei; Bai, Keke; Li, Hui

2013-01-01

3-Oxotabersonine (OTAB) is a component of Voacanga africana, which is a type of traditional drug in Africa widely used for treating diseases. This study examines the interaction of OTAB with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions. The interaction between OTAB and BSA/HSA was investigated using fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, circular dichroism (CD) spectroscopy, and molecular modeling under simulated physiological conditions. The experimental results confirm that the quenching mechanism is a static quenching process. The binding site number (n) and the apparent binding constant (K) were measured at various temperatures. The thermodynamic parameters, namely, enthalpy change (ΔH) and entropy change (ΔS), were calculated. Furthermore, the structural changes in the serum albumin that affected the OTAB binding were determined using FT-IR. The binding site was assumed to be located in site I of the BSA/HSA (subdomain IIA). -- Highlights: ► Make use of the 3-Oxotabersonine firstly extracted from seeds of Voacanga africana Stapf to study the drug–protein system. ► Use two kinds of similar structure serum albumins to do a comparative study. ► FT-IR was used to study the conformational change of BSA and HSA. ► Use the BSA and HSA structure obtained from the Brookhaven Protein Data Bank for molecular docking

Characterization of the interaction between 3-Oxotabersonine and two serum albumins by using spectroscopic techniques

Energy Technology Data Exchange (ETDEWEB)

Wang, Qing; Yan, Jin; He, Jiawei; Bai, Keke [College of Chemical Engineering, Sichuan University, Chengdu 610065 (China); Li, Hui, E-mail: lihuilab@sina.com [College of Chemical Engineering, Sichuan University, Chengdu 610065 (China)

2013-06-15

3-Oxotabersonine (OTAB) is a component of Voacanga africana, which is a type of traditional drug in Africa widely used for treating diseases. This study examines the interaction of OTAB with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions. The interaction between OTAB and BSA/HSA was investigated using fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, circular dichroism (CD) spectroscopy, and molecular modeling under simulated physiological conditions. The experimental results confirm that the quenching mechanism is a static quenching process. The binding site number (n) and the apparent binding constant (K) were measured at various temperatures. The thermodynamic parameters, namely, enthalpy change (ΔH) and entropy change (ΔS), were calculated. Furthermore, the structural changes in the serum albumin that affected the OTAB binding were determined using FT-IR. The binding site was assumed to be located in site I of the BSA/HSA (subdomain IIA). -- Highlights: ► Make use of the 3-Oxotabersonine firstly extracted from seeds of Voacanga africana Stapf to study the drug–protein system. ► Use two kinds of similar structure serum albumins to do a comparative study. ► FT-IR was used to study the conformational change of BSA and HSA. ► Use the BSA and HSA structure obtained from the Brookhaven Protein Data Bank for molecular docking.

Nanoparticle albumin-bound paclitaxel: a novel Cremphor-EL-free formulation of paclitaxel.

Science.gov (United States)

Stinchcombe, Thomas E

2007-08-01

Standard formulation paclitaxel requires the use of solvents, such as Cremphor-EL, which contribute to some of the toxicities commonly associated with paclitaxel-based therapy. Nanoparticle albumin-bound paclitaxel (nab-paclitaxel) is a novel solvent-free formulation of paclitaxel. The formulation is prepared by high-pressure homogenization of paclitaxel in the presence of serum albumin into a nanoparticle colloidal suspension. The human albumin-stabilized paclitaxel particles have an average size of 130 nm. Nab-paclitaxel has several practical advantages over Cremphor-EL-paclitaxel, including a shorter infusion time (30 min) and no need for premedications for hypersensitivity reactions. The nab-paclitaxel formulation eliminates the impact of Cremphor-EL on paclitaxel pharmacokinetics and utilizes the endogenous albumin transport mechanisms to concentrate nab-paclitaxel within the tumor. A recent Phase III trial compared nab- and Cremphor-EL-paclitaxel in patients with metastatic breast cancer. Patients treated with nab-paclitaxel experienced a higher response, longer time to tumor progression and, in patients receiving second-line or greater therapy, a longer median survival. Patients treated with nab-paclitaxel had a significantly lower rate of severe neutropenia and a higher rate of sensory neuropathy. The preclinical and clinical data indicate that the nab-paclitaxel formulation has significant advantages over Cremphor-EL-paclitaxel.

A novel technology using transscleral ultrasound to deliver protein loaded nanoparticles.

Science.gov (United States)

Huang, Di; Wang, Lili; Dong, Yixuan; Pan, Xin; Li, Ge; Wu, Chuanbin

2014-09-01

This study was designed to investigate the feasibility of silk fibroin nanoparticles (SFNs) for sustained drug delivery in transscleral ultrasound. Fluorescein isothiocynate labeled bovine serum albumin (FITC-BSA, MW 66.45 kDa) was chosen as a model macromolecular protein drug and SFNs were used as nano-carrier systems suitable for ocular drug delivery. Drug loaded nanoparticles (FITC-BSA-SFNs) were first prepared and characterized. In vitro transscleral study under ultrasound exposure (1MHz, 0.5 W/cm(2), 5 min continuous wave) using isolated sclera of rabbit was performed. The posterior eye segment of rabbit was examined for adverse effect by slit-lamp and histology. It was found that FITC-BSA-SFNs possessed sustained release, bioadhesive, and co-permeation characteristics. The ultrasound application significantly improved the penetration efficiency of FITC-BSA-SFNs as compared with passive delivery, meanwhile caused no damages to the ocular tissue and particles themselves. The distribution profile of SFNs revealed rapid and lasting adhesion on the outer scleral tissues, followed by migration into the interior up to one week after treatment. This research suggested a novel non-invasive transscleral administration of macromolecular protein drugs using SFN carriers combining with ultrasound technology. Copyright © 2014 Elsevier B.V. All rights reserved.

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)

Chen, Lijian; Wang, Nan; Wang, Xindong; Ai, Shiyun

2013-01-01

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)

A multispectroscopic and molecular docking investigation of the binding interaction between serum albumins and acid orange dye

Science.gov (United States)

Naveenraj, Selvaraj; Solomon, Rajadurai Vijay; Mangalaraja, Ramalinga Viswanathan; Venuvanalingam, Ponnambalam; Asiri, Abdullah M.; Anandan, Sambandam

2018-03-01

The interaction of Acid Orange 10 (AO10) with bovine serum albumin (BSA) was investigated comparatively with that of human serum albumin (HSA) using multispectroscopic techniques for understanding their toxic mechanism. Further, density functional theory calculations and docking studies have been carried out to gain more insights into the nature of interactions existing between AO10 and serum albumins. The fluorescence results suggest that AO10 quenched the fluorescence of BSA through the combination of static and dynamic quenching mechanism. The same trend was followed in the interaction of AO10 with HSA. In addition to the type of quenching mechanism, the fluorescence spectroscopic results suggest that the binding occurs near the tryptophan moiety of serum albumins and the binding. AO10 has more binding affinity towards BSA than HSA. An AO10-Trp model has been created to explicitly understand the Csbnd Htbnd π interactions from Bader's quantum theory of atoms in molecules analysis which confirmed that AO10 bind more strongly with BSA than that of HSA due to the formation of three hydrogen bonds with BSA whereas it forms two hydrogen bonds in the case of HSA. These obtained results provide an in-depth understanding of the interaction of the acid azo dye AO10 with serum albumins. This interaction study provides insights into the underlying reasons for toxicity of AO10 relevant to understand its effect on bovids and humans during the blood transportation process.

[Spectroscopic studies on the interaction of nicotine and BSA].

Science.gov (United States)

Chen, Yun; Kong, Xiang-rong; Shen, Xinag-can; Liang, Hong

2005-10-01

The interaction of nicotine and bovine serum albumin(BSA) was investigated by fluorescence spectra and UV-vis spectra. The fluorescence spectrum showed that BSA fluorescence quench regularly with the addition of nicotine.The fluorescence quenching mechanisms were also studied in pH 5.0, pH 7.4 and pH 11.0 by Stern-Volmer equation, indicating dynamic quenching(pH 5.0) and static quenching(pH 7.4 and pH 11.0) respectively. Association constants (k) of nicotine and BSA at pH 7.4 and pH 11.0 at the temperatures of 20 and 37 degrees C were given by the Lineweaver-Buck equation, which are: k(20 degrees C) = 140.15 L x mol(-1) and k(37 degrees C) = 131.83 mol x L(-1) (pH 7.4), and k(20 degrees C) = 141.76 mol x L(-1), k(37 degrees C) = 27.79 mol x L(-1) (pH 11.0), suggesting that the association constant is effected by the temperature much more remarkably at pH 7.4 than that at pH 11.0 because of the different states of nicotine at different pHs. The UV-Vis spectra exhibit that the absorbance of BSA(210 nm) shifts to red and decreases gradually with the addition of nicotine, reflecting the transition of secondary structure of BSA, namely, the helix of BSA becomes looser. The UV-Vis second derivative spectra and synchronous spectra (delta wavelength = wavelength(em) - wavelength(ex) = 15 nm and delta wavelength = wavelength(em) - wavelength(ex) = 60 nm) imply the change of the microcircumstance of aromatic amino residues of BSA(Trp, Tyr and Phe) from hydrophobicity to hydrophilicity at high concentration of nicotine.

Ligand-Modified Human Serum Albumin Nanoparticles for Enhanced Gene Delivery.

Science.gov (United States)

Look, Jennifer; Wilhelm, Nadine; von Briesen, Hagen; Noske, Nadja; Günther, Christine; Langer, Klaus; Gorjup, Erwin

2015-09-08

The development of nonviral gene delivery systems is a great challenge to enable safe gene therapy. In this study, ligand-modified nanoparticles based on human serum albumin (HSA) were developed and optimized for an efficient gene therapy. Different glutaraldehyde cross-linking degrees were investigated to optimize the HSA nanoparticles for gene delivery. The peptide sequence arginine-glycine-aspartate (RGD) and the HIV-1 transactivator of transduction sequence (Tat) are well-known as promising targeting ligands. Plasmid DNA loaded HSA nanoparticles were covalently modified on their surface with these different ligands. The transfection potential of the obtained plasmid DNA loaded RGD- and Tat-modified nanoparticles was investigated in vitro, and optimal incubation conditions for these preparations were studied. It turned out that Tat-modified HSA nanoparticles with the lowest cross-linking degree of 20% showed the highest transfection potential. Taken together, ligand-functionalized HSA nanoparticles represent promising tools for efficient and safe gene therapy.

Nanocomposite materials based on poly(vinyl chloride) and bovine serum albumin modified ZnO through ultrasonic irradiation as a green technique: Optical, thermal, mechanical and morphological properties.

Science.gov (United States)

Mallakpour, Shadpour; Darvishzadeh, Marzieh

2018-03-01

In this project, physicochemical properties of poly(vinyl chloride) (PVC) reinforced by ZnO nanoparticles (NPs) were studied. Firstly, ZnO NPs were modified with bovine serum albumin (BSA) as an organo-modifier and biocompatible substance through ultrasound irradiation as environmental friendly, low cost and rapid means. Nanocomposite (NC) films were prepared by loadings of various ratios of ZnO/BSA NPs (3, 6 and 9wt%) inside the PVC. Structural morphology and physical properties of the ZnO-BSA NPs and NC films were investigated via Fourier transform infrared spectroscopy, X-ray diffraction, thermogravimetric analysis (TGA), transmission electron microscopy and field emission scanning electron microscopy. According to the obtained information from the TGA, an increase in the thermal stability can be clearly observed. Also the results of contact angle analysis indicated with increasing percent of ZnO/BSA NPs into PVC the hydrophilic behaviors of NCs were increased. Copyright © 2017 Elsevier B.V. All rights reserved.

[Binding interaction of harpagoside and bovine serum albumin: spectroscopic methodologies and molecular docking].

Science.gov (United States)

Cao, Tuan-Wu; Huang, Wen-Bing; Shi, Jian-Wei; He, Wei

2018-03-01

Scrophularia ningpoensis has exhibited a variety of biological activities and been used as a pharmaceutical product for the treatment of inflammatory ailment, rheumatoid arthritis, osteoarthritis and so on. Harpagoside (HAR) is considerer as a main bioactive compound in this plant. Serum albumin has important physiological roles in transportation, distribution and metabolism of many endogenous and exogenous substances in body. It is of great significance to study the interaction mechanism between HAR and bovine serum albumin (BSA). The mechanism of interaction between HAR and BSA was investigated using 2D and 3D fluorescence, synchronous florescence, ultraviolet spectroscopy and molecular docking. According to the analysis of fluorescence spectra, HAR could strongly quench the fluorescence of BSA, and the static quenching process indicated that the decrease in the quenching constant was observed with the increase in temperature. The magnitude of binding constants (KA) was more than 1×10⁵ L·mol⁻¹, and the number of binding sites(n) was approximate to 1. The thermodynamic parameters were calculated through analysis of fluorescence data with Stern-Volmer and Van't Hoff equation. The calculated enthalpy change (ΔH) and entropy change (ΔS) implied that the main interaction forces of HAR with BSA were the bonding interaction between van der Waals forces and hydrogen. The negative values of energy (ΔG) demonstrated that the binding of HAR with BSA was a spontaneous and exothermic process. The binding distance(r) between HAR and BSA was calculated to be about 2.80 nm based on the theory of Frster's non-radiation energy transfer, which indicated that energy is likely to be transfer from BSA to HAR. Both synchronous and 3D florescence spectroscopy clearly revealed that the microenvironment and conformation of BSA changed during the binding interaction between HAR and BSA. The molecular docking analysis revealed HAR is more inclined to BSA and human serum albumin

Determination of the activity of telomerase in cancer cells by using BSA-protected gold nanoclusters as a fluorescent probe.

Science.gov (United States)

Xu, Yujuan; Zhang, Peng; Wang, Zhen; Lv, Shaoping; Ding, Caifeng

2018-02-27

Gold nanoclusters (AuNCs) protected with a bovine serum albumin (BSA) coating are known to emit red fluorescence (peaking at 650 nm) on photoexcitation with ultraviolet light (365 nm). On addition of Cu(II) ions, fluorescence is quenched because Cu(II) complexes certain amino acid units in the BSA chain. Fluorescence is, however, restored if pyrophosphate (PPi) is added because it will chelate Cu(II) and remove it from the BSA coating on the AuNCs. Because PPi is involved in the function of telomerase, the BSA@AuNCs loaded with Cu(II) can act as a fluorescent probe for determination of the activity of telomerase. A fluorescent assay was worked out for telomerase that is highly sensitive and has a wide linear range (10 nU to 10 fM per mL). The fluorescent probe was applied to the determination of telomerase activity in cervix carcinoma cells via imaging. It is shown that tumor cells can be well distinguished from normal cells by monitoring the differences in intracellular telomerase activity. Graphical abstract Gold nanoclusters (AuNCs) protected by bovine serum albumin (BSA) and displaying red photoluminescence were prepared as fluorescent probe for the determination of telomerase activity and used for imaging of cervix carcinoma (HeLa) cells.

Study on the Interaction between Cadmium Sulphide Nanoparticles and Proteins by Resonance Rayleigh Scattering Spectra

Directory of Open Access Journals (Sweden)

Weiwei Zhu

2013-01-01

Full Text Available The interaction of cadmium sulphide nanoparticles [(CdSn] with proteins has been studied by resonance Rayleigh scattering spectra (RRS. Below the isoelectric point, proteins such as bovine serum albumin (BSA, human serum albumin (HSA, lysozyme (Lys, hemoglobin (HGB, and ovalbumin (OVA can bind with CdSn to form macromolecules by virtue of electrostatic attraction and hydrophobic force. It can result in the enhancement of resonance Rayleigh scattering spectra (RRS intensity. Their maximum scattering peaks were 280 nm, and there was a smaller peak at 370 nm. The scattering enhancement (ΔIRRS is directly proportional to the concentration of proteins. A new RRS method for the determination of trace proteins using uncapped CdSn nanoparticles probe has been developed. The detection limits are 19.6 ng/mL for HSA, 16.7 ng/mL for BSA, 18.5 ng/mL for OVA, 80.2 ng/mL for HGB, and 67.4 ng/mL for Lys, separately. In this work, the optimum condition of reaction, the effect of foreign, and the analytical application had been investigated.

The effect of glycation on bovine serum albumin conformation and ligand binding properties with regard to gliclazide

Science.gov (United States)

Żurawska-Płaksej, Ewa; Rorbach-Dolata, Anna; Wiglusz, Katarzyna; Piwowar, Agnieszka

2018-01-01

Albumin, the major serum protein, plays a variety of functions, including binding and transporting endogenous and exogenous ligands. Its molecular structure is sensitive to different environmental modifiers, among which glucose is one of the most significant. In vivo albumin glycation occurs under physiological conditions, but it is increased in diabetes. Since bovine serum albumin (BSA) may serve as a model protein in in vitro experiments, we aimed to investigate the impact of glucose-mediated BSA glycation on the binding capacity towards gliclazide, as well as the ability of this drug to prevent glycation of the BSA molecule. To reflect normo- and hyperglycemia, the conditions of the glycation process were established. Structural changes of albumin after interaction with gliclazide (0-14 μM) were determined using fluorescence quenching and circular dichroism spectroscopy. Moreover, thermodynamic parameters as well as energy transfer parameters were determined. Calculated Stern-Volmer quenching constants, as well as binding constants for the BSA-gliclazide complex, were lower for the glycated form of albumin than for the unmodified protein. The largest, over 2-fold, decrease in values of binding parameters was observed for the sample with 30 mM of glucose, reflecting the poorly controlled diabetic state, which indicates that the degree of glycation had a critical influence on binding with gliclazide. In contrast to significant changes in the tertiary structure of BSA upon binding with gliclazide, only slight changes in the secondary structure were observed, which was reflected by about a 3% decrease of the α-helix content of glycated BSA (regardless of glucose concentration) in comparison to unmodified BSA. The presence of gliclazide during glycation did not affect its progress. The results of this study indicate that glycation significantly changed the binding ability of BSA towards gliclazide and the scale of these changes depended on glucose concentration. It

Structural changes during the unfolding of Bovine serum albumin

Indian Academy of Sciences (India)

The native form of serum albumin is the most important soluble protein in the body plasma. In order to investigate the structural changes of Bovine serum albumin (BSA) during its unfolding in the presence of urea, a small-angle neutron scattering (SANS) study was performed. The scattering curves of dilute solutions of BSA ...

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.

Coating of gold nanoparticles for medical application: UV-VIS

Science.gov (United States)

Martínez Espinosa, Juan Carlos; Ramírez, Nayem Amtanus Chequer; Funes Oliva, Luis Enrique; Córdova Fraga, Teodoro; Bernal Alvarado, Jesús; Reyes Pablo, Aldelmo; Núñez, Anita Rosa Elvira

2014-11-01

The use of nanostructured materials has gained strength in recent years in the biomedical area; new applications such as the detection of components in living cells have been used in pharmaceutical area, specifically to study the interaction of various antitumor drugs in living tissues, the detection of genes that are closely related to some type of cancer, as well as the detections of protein biomarkers for diseases also have been studied in various research laboratories around of the world. In this work, we characterize the variation of the absorbance of gold nanoparticles (GNPs) coated with different concentration of Bovine Serum Albumin (BSA) protein. We use GNPS of 60 nm of the trademark-TED PELLA, the BSA protein trademark of Sigma Aldrich and based on that proposed protocol by Chithrani et al., 2009 with purposes to obtain an alternative model to determine the optimal stability of the nanoparticles coated with the protein. The colloidal solutions were prepared with BSA at different concentrations (0.25, 0.5, 0.75 and 1% M/V), and were centrifuged at 15,000 rpm for 90 minutes (centrifuge Model Z383K) and a constant temperature of 25 °C. All the spectra sets were obtained within the range from 400 to 700 nm using an UV-VIS spectrophotometer (Thermo Scientific Model 51118650). The results showed a R2 of 0.99 for an exponential curve correlation between the concentration of BSA, and the absorbance measured. We found at higher concentrations of BSA, there is a decrease in the intensity of the absorption spectra in the plasmon resonance. This preliminary model obtained can be used in the stabilization of gold nanoparticles with different proteins of biomedical interest in future experiments and support for functionalization of GNPs with specific membrane markers.

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

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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.

An albumin-based gold nanocomposites as potential dual mode CT/MRI contrast agent

Science.gov (United States)

Zhao, Wenjing; Chen, Lina; Wang, Zhiming; Huang, Yuankui; Jia, Nengqin

2018-02-01

In pursuit of the biological detection applications, recent years have witnessed the prosperity of novel multi-modal nanoprobes. In this study, biocompatible bovine serum albumin (BSA)-coated gold nanoparticles (Au NPs) containing Gd (III) as the contrast agent for both X-ray CT and T1-weighted MR imaging is reported. Firstly, the Au NPs with BSA coating (Au@BSA) was prepared through a moderate one-pot reduction route in the presence of hydrazine hydrate as reducer. Sequentially, the BSA coating enables modification of diethylenetriaminepentaacetic acid (DTPA) as well as targeting reagent hyaluronic acid (HA), and further chelation of Gd (III) ions led to the formation of biomimetic nanoagent HA-targeted Gd-Au NPs (HA-targeted Au@BSA-Gd-DTPA). Several techniques were used to thoroughly characterize the formed HA-targeted Gd-Au NPs. As expected, the as-prepared nanoagent with mean diameter of 13.82 nm exhibits not only good colloid stablility and water dispersibility, but also satisfying low cytotoxicity and hemocompatibility in the tested concentration range. Additionally, for the CT phantoms, the obtained nanocomplex shows an improved contrast in CT scanning than that of Au@BSA as well as small molecule iodine-based CT contrast agents such as iopromide. Meanwhile, for the T1-weighted MRI images, there is a linear increase of contrast with concentration of Gd for the two cases of HA-targeted Gd-Au NPs and Magnevist. Strikingly, the nanoagent we explored displays a relatively higher r1 relaxivity than that of commercial MR contrast agents. Therefore, this newly constructed nanoagent could be used as contrast agents for synergistically enhanced X-ray CT and MR phantoms, holding promising potential for future biomedical applications.

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

International Nuclear Information System (INIS)

Shi Xiaolei; Li Xuwen; Gui Mingyu; Zhou Hongyu; Yang Ruijie; Zhang Hanqi; Jin Yongri

2010-01-01

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.

Adsorption of acidic, basic, and neutral proteins from aqueous samples using Fe3O4 magnetic nanoparticles modified with an ionic liquid

International Nuclear Information System (INIS)

Kamran, S.; Asadi, M.; Absalan, G.

2013-01-01

We have prepared and characterized Fe 3 O 4 nanoparticles and their binary mixtures (IL-Fe 3 O 4 ) with 1-hexyl-3-methylimidazolium bromide as ionic liquid for use in the adsorption of lysozyme (LYS), bovine serum albumin (BSA), and myoglobin (MYO). The optimum operational conditions for the adsorption of proteins (at 0.05-2.0 mg mL -1 ) were 4.0 mg mL -1 of nanoparticles and a contact time of 10 min. The maximum adsorption capacities are 455, 182 and 143 mg for LYS, BSA, and MYO per gram of adsorbent, respectively. The Langmuir model better fits the adsorption isotherms, with adsorption constants of 0.003, 0.015 and 0.008 L mg -1 , in order, for LYS, BSA, MYO. The applicability of two kinetic models including pseudo-first order and pseudo-second order model was estimated on the basis of comparative analysis of the corresponding rate parameters, equilibrium adsorption capacity and correlation coefficients. The adsorption processes are endothermic. The proteins can be desorbed from the nanoparticles by using NaCl solution at pH 9.5, and the nanoparticles thus can be recycled. (author)

Biomimetic synthesis of calcium carbonate with different morphologies and polymorphs in the presence of bovine serum albumin and soluble starch.

Science.gov (United States)

Liu, Yuxi; Chen, Yuping; Huang, Xuechen; Wu, Gang

2017-10-01

Calcium carbonate has been synthesized by the reaction of Na 2 CO 3 and CaCl 2 in the presence of bovine serum albumin (BSA) and soluble starch. Effects of various bovine serum albumin (BSA) and soluble starch on the polymorph and morphology of CaCO 3 crystals were investigated. Crystallization of vaterite is favored in the presence of BSA and soluble starch, respectively, while calcite is favored in the presence of a mixture of BSA and soluble starch. The morphologies of CaCO 3 particles in the presence of mixture of BSA and soluble starch are mainly rod-like, suggesting that the BSA, soluble and their assemblies play key roles in stabilizing and directing the CaCO 3 crystal growth. Copyright © 2017. Published by Elsevier B.V.

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

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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.

BSA treatment to enhance enzymatic hydrolysis of cellulose in lignin containing substrates.

Science.gov (United States)

Yang, Bin; Wyman, Charles E

2006-07-05

Cellulase and bovine serum albumin (BSA) were added to Avicel cellulose and solids containing 56% cellulose and 28% lignin from dilute sulfuric acid pretreatment of corn stover. Little BSA was adsorbed on Avicel cellulose, while pretreated corn stover solids adsorbed considerable amounts of this protein. On the other hand, cellulase was highly adsorbed on both substrates. Adding a 1% concentration of BSA to dilute acid pretreated corn stover prior to enzyme addition at 15 FPU/g cellulose enhanced filter paper activity in solution by about a factor of 2 and beta-glucosidase activity in solution by about a factor of 14. Overall, these results suggested that BSA treatment reduced adsorption of cellulase and particularly beta-glucosidase on lignin. Of particular note, BSA treatment of pretreated corn stover solids prior to enzymatic hydrolysis increased 72 h glucose yields from about 82% to about 92% at a cellulase loading of 15 FPU/g cellulose or achieved about the same yield at a loading of 7.5 FPU/g cellulose. Similar improvements were also observed for enzymatic hydrolysis of ammonia fiber explosion (AFEX) pretreated corn stover and Douglas fir treated by SO(2) steam explosion and for simultaneous saccharification and fermentation (SSF) of BSA pretreated corn stover. In addition, BSA treatment prior to hydrolysis reduced the need for beta-glucosidase supplementation of SSF. The results are consistent with non-specific competitive, irreversible adsorption of BSA on lignin and identify promising strategies to reduce enzyme requirements for cellulose hydrolysis. (c) 2006 Wiley Periodicals, Inc.

Spectroscopic studies on the interaction of mimosine with BSA and DNA

Science.gov (United States)

Baltazar, C. J.; Mun, R.; Tajmir-Riahi, H. A.; Bariyanga, J.

2018-06-01

Mimosine has shown antitumor activity towards cancer cells. It has also been found to inhibit deoxyribonucleic acid (DNA) but the interaction is not fully understood. Here we report the results of investigation of its interactions with bovine serum albumin (BSA) and DNA in aqueous solution (pH 7.4) using FTIR and UV spectroscopic methods. Mimosine was found to disrupt the conformation of BSA by reducing its α-helix component and promoting a partial unfolding of the protein. In addition, the results indicated that mimosine may bind to DNA by electrostatic attractions via phosphate groups and grooves. The overall binding constant of DNA -mimosine complex was 5 × 10 3 M-1.

Human Albumin Fragments Nanoparticles as PTX Carrier for Improved Anti-cancer Efficacy

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Liang Ge

2018-06-01

Full Text Available For enhanced anti-cancer performance, human serum albumin fragments (HSAFs nanoparticles (NPs were developed as paclitaxel (PTX carrier in this paper. Human albumins were broken into fragments via degradation and crosslinked by genipin to form HSAF NPs for better biocompatibility, improved PTX drug loading and sustained drug release. Compared with crosslinked human serum albumin NPs, the HSAF-NPs showed relative smaller particle size, higher drug loading, and improved sustained release. Cellular and animal results both indicated that the PTX encapsulated HSAF-NPs have shown good anti-cancer performance. And the anticancer results confirmed that NPs with fast cellular internalization showed better tumor inhibition. These findings will not only provide a safe and robust drug delivery NP platform for cancer therapy, but also offer fundamental information for the optimal design of albumin based NPs.

The effect of paracetamol on 5 fluorouracil and bovine serum albumin interaction: A biophysical study

Science.gov (United States)

Dahiya, Vandana; Pal, Samanwita

2018-05-01

Serum Albumin is a major carrier protein and its binding with drugs is important to examine the change in pharmacokinetic properties due to interaction amongst drugs. In the present study we have attempted to understand the relevant drug-drug interaction (DDI) between two common drugs viz, paracetamol, an anti-inflammatory and fluorouracil, an anti-cancer drug. In-vitro spectroscopic methods viz., fluorescence quenching and UV-vis absorption have been employed for the drug-bovine serum albumin (BSA) complexes studies. The binding parameters and quenching constants have been determined for BSA-Paracetamol and BSA-5Fluorouracil complex according to literature models. It is also predicted from the quenching studies that BSA-5Fluorouracil is a stronger complex than BSA-Paracetamol. On the other hand paracetamol can alter binding affinity of 5Fluorouracil towards BSA. Hence it becomes clear that although the drugs could be administered simultaneously but they influence each other's binding with protein in a concentration dependent fashion. Further these results also indicate that availability of free 5Fluorouracil in blood may increase in presence of paracetamol.

Thermo-responsive human α-elastin self-assembled nanoparticles for protein delivery.

Science.gov (United States)

Kim, Jae Dong; Jung, Youn Jae; Woo, Chang Hee; Choi, Young Chan; Choi, Ji Suk; Cho, Yong Woo

2017-01-01

Self-assembled nanoparticles based on PEGylated human α-elastin were prepared as a potential vehicle for sustained protein delivery. The α-elastin was extracted from human adipose tissue and modified with methoxypolyethyleneglycol (mPEG) to control particle size and enhance the colloidal stability. The PEGylated human α-elastin showed sol-to-particle transition with a lower critical solution temperature (LCST) of 25°C-40°C in aqueous media. The PEGylated human α-elastin nanoparticles (PhENPs) showed a narrow size distribution with an average diameter of 330±33nm and were able to encapsulate significant amounts of insulin and bovine serum albumin (BSA) upon simple mixing at low temperature in water and subsequent heating to physiological temperature. The release profiles of insulin and BSA showed sustained release for 72h. Overall, the thermo-responsive self-assembled PhENPs provide a useful tool for a range of protein delivery and tissue engineering applications. Copyright © 2016 Elsevier B.V. All rights reserved.

Preparation of Curcumin Loaded Egg Albumin Nanoparticles Using Acetone and Optimization of Desolvation Process.

Science.gov (United States)

Aniesrani Delfiya, D S; Thangavel, K; Amirtham, D

2016-04-01

In this study, acetone was used as a desolvating agent to prepare the curcumin-loaded egg albumin nanoparticles. Response surface methodology was employed to analyze the influence of process parameters namely concentration (5-15%w/v) and pH (5-7) of egg albumin solution on solubility, curcumin loading and entrapment efficiency, nanoparticles yield and particle size. Optimum processing conditions obtained from response surface analysis were found to be the egg albumin solution concentration of 8.85%w/v and pH of 5. At this optimum condition, the solubility of 33.57%, curcumin loading of 4.125%, curcumin entrapment efficiency of 55.23%, yield of 72.85% and particles size of 232.6 nm were obtained and these values were related to the values which are predicted using polynomial model equations. Thus, the model equations generated for each response was validated and it can be used to predict the response values at any concentration and pH.

Surface functionalization of zirconium dioxide nano-adsorbents with 3-aminopropyl triethoxysilane and promoted adsorption activity for bovine serum albumin

Energy Technology Data Exchange (ETDEWEB)

Liu, Gen; Wu, Chaochao [Department of Chemistry, College of Sciences, Northeastern University, Shenyang 110819 (China); Zhang, Xia, E-mail: xzhang@mail.neu.edu.cn [Department of Chemistry, College of Sciences, Northeastern University, Shenyang 110819 (China); Liu, Yufeng, E-mail: liuyufeng@bjmu.edu.cn [College of Pharmacy, Liaoning University, Shenyang 110036 (China); Meng, Hao; Xu, Junli; Han, Yide; Xu, Xinxin; Xu, Yan [Department of Chemistry, College of Sciences, Northeastern University, Shenyang 110819 (China)

2016-06-15

Surface functionalization of zirconium dioxide (ZrO{sub 2}) nano-adsorbents was carried out by using 3-aminopropyl triethoxysilane (APTES) as the modifier. The addition amount of APTES was varied to determine the optimum modification extent, and the bulk ZrO{sub 2} microparticles were also modified by APTES for comparison. Some means, such as TEM, XRD, FT-IR, XPS and TG-DSC were used to character these ZrO{sub 2} particles. The results showed that the APTES molecules were chemically immobilized on the surface of ZrO{sub 2} nanoparticles via Zr−O−Si bonds, and the nano-ZrO{sub 2} samples showed larger special surface area. In the adsorption of bovine serum albumin (BSA), nano-ZrO{sub 2} samples exhibited enhanced adsorption activity, and APTES modified nano-ZrO{sub 2} with proper APTES content presented the best adsorption property. Under the same adsorption conditions, the equilibrium adsorption capacity of BSA on APTES-ZrO{sub 2}-2 was almost 2.3 times as that on pristine nano-ZrO{sub 2} and 3.0 times as on bulk ZrO{sub 2} microparticles. The increased adsorption capacity of APTES-ZrO{sub 2} nano-adsorbents can be attributed to the chemical interaction between amino and carboxyl groups at APTES-ZrO{sub 2}/BSA interface. The pH-dependent experiments showed that the optimum pH value for the adsorption and desorption was 5.0 and 9.0, respectively, which suggested that the adsorption and release of BSA could be controlled simply by adjusting the solution pH condition. - Highlights: • APTES chemically immobilized on ZrO{sub 2} nanoparticles via Zr−O−Si bond. • Enhanced adsorption capacity of BSA was observed on APTES-ZrO{sub 2}. • Chemical adsorption character of BSA on APTES-ZrO{sub 2}. • Adsorption/release of BSA on APTES-ZrO{sub 2} accomplished by adjusting pH value.

Nanoparticle Albumin-Bound-Paclitaxel in the Treatment of Metastatic Urethral Adenocarcinoma: The Significance of Molecular Profiling and Targeted Therapy

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Yasmin M. Abaza

2014-01-01

Full Text Available Primary urethral cancer is rare and accounts for only 0.003% of all malignancies arising from the female genitourinary tract. Due to the rarity of this disease, no consensus exists regarding the optimal therapeutic approach. Nanoparticle albumin-bound-paclitaxel has been shown to be effective in the treatment of a number of malignancies including metastatic breast, pancreatic, and bladder cancer. We present a 67-year-old woman with advanced metastatic urethral adenocarcinoma resistant to two lines of chemotherapy (ifosfamide/paclitaxel/cisplatin and irinotecan/5-fluorouracil/leucovorin that showed a dramatic response to nanoparticle albumin-bound-paclitaxel. This is the first case report to document the use and efficacy of nanoparticle albumin-bound-paclitaxel in the treatment of unresectable metastatic urethral cancer.

Determination of association constants between steroid compounds and albumins by partial-filling ACE.

Science.gov (United States)

Amundsen, Lotta K; Sirén, Heli

2007-10-01

ACE is a popular technique for evaluating association constants between drugs and proteins. However, ACE has not previously been applied to study the association between electrically neutral biomolecules and plasma proteins. We studied the affinity between human and bovine serum albumins (HSA and BSA, respectively) and three neutral endogenous steroid hormones (testosterone, epitestosterone and androstenedione) and two synthetic analogues (methyltestosterone and fluoxymesterone) by applying the partial-filling technique in ACE (PF-ACE). From the endocrinological point of view, the distribution of endogenous steroids among plasma components is of great interest. Strong interactions with albumins suppress the biological activity of steroids. Notable differences in the association constants were observed. In the case of the endogenous steroids, the interactions between testosterone and the albumins were strongest, and those between androstenedione and the albumins were substantially weaker. The association constants, K(b), for testosterone, epitestosterone and androstenedione and HSA at 37 degrees C were 32 100 +/- 3600, 21 600 +/- 1500 and 13 300 +/- 1300 M(-1), respectively, while the corresponding values for the steroids and BSA were 18 800 +/- 1500, 14 000 +/- 400 and 7800 +/- 900 M(-1). Methyltestosterone was bound even more strongly than testosterone, while fluoxymesterone was only weakly bound by the albumins. Finally, the steroids were separated by PF-ACE with HSA and BSA used as resolving components.

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

Energy Technology Data Exchange (ETDEWEB)

Selva Sharma, Arumugam [Department of Chemistry, Bharathiar University, Coimbatore 641046 (India); Anandakumar, Shanmugam [Department of Bioinformatics, Bharathiar University, Coimbatore 641046 (India); Ilanchelian, Malaichamy, E-mail: chelian73@yahoo.com [Department of Chemistry, Bharathiar University, Coimbatore 641046 (India)

2014-07-01

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.

Preparation, structural analysis and bioactivity of ribonuclease A-albumin conjugate: tetra-conjugation or PEG as the linker.

Science.gov (United States)

Li, Chunju; Lin, Qixun; Wang, Jun; Shen, Lijuan; Ma, Guanghui; Su, Zhiguo; Hu, Tao

2012-12-31

Ribonuclease A (RNase A) is a therapeutic enzyme with cytotoxic action against tumor cells. Its clinical application is limited by the short half-life and insufficient stability. Conjugation of albumin can overcome the limitation, whereas dramatically decrease the enzymatic activity of RNase A. Here, three strategies were proposed to prepare the RNase A-bovine serum albumin (BSA) conjugates. R-SMCC-B (a conjugate of four RNase A attached with one BSA) and R-PEG-B (a mono-conjugate) were prepared using Sulfo-SMCC (a short bifunctional linker) and mal-PEG-NHS (a bifunctional PEG), respectively. Mal-PEG-NHS and hexadecylamine (HDA) were used to prepare the mono-conjugate, R-HDA-B, where HDA was adopted to bind BSA. The PEG linker can elongate the proximity between RNase A and BSA. In contrast, four RNase A were closely located on BSA in R-SMCC-B. R-SMCC-B showed the lowest K(m) and the highest relative enzymatic activity and k(cat)/K(m) in the three conjugates. Presumably, the tetravalent interaction of RNase A in R-SMCC-B can increase the binding affinity to its substrate. In addition, the slow release of BSA from R-HDA-B may increase the enzymatic activity of R-HDA-B. Our study is expected to provide strategies to develop protein-albumin conjugate with high therapeutic potential. Copyright © 2012 Elsevier B.V. All rights reserved.

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

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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.

Interactions of cephalexin with bovine serum albumin: displacement reaction and molecular docking

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Hamed Hamishehkar

2016-09-01

Conclusion: The outcomes of spectroscopic methods revealed that the conformation of BSA changed during drug-BSA interaction. The results of FRET propose that CPL quenches the fluorescence of BSA by static quenching and FRET. The displacement study showed that phenylbutazon and ketoprofen displaced CPL, indicating that its binding site on albumin is site I and Gentamicin cannot be displaced from the binding site of CPL. All results of molecular docking method agreed with the results of experimental data.

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.

Bovine serum albumin adsorption on passivated porous silicon layers

Science.gov (United States)

Lockwood, David; Boukherroub, Rabah

2005-03-01

Hydrogen-terminated porous silicon (pSi) films were fabricated through electrochemical anodization of crystalline Si in HF-based solutions. The pSi-H surface was chemically functionalized by thermal reaction with undecylenic acid to produce an organic monolayer covalently attached to the silicon surface through Si-C bonds and bearing an acid terminal group. Bovine serum albumin (BSA) was then adsorbed onto the modified surface. SEM showed that the porous films were damaged and partially lifted off the Si substrate after a prolonged BSA adsorption. Ellipsometry revealed that the BSA had penetrated ˜ 1.3 micrometers into the porous structure. The film damage results from BSA anchoring itself tightly through strong electrostatic interactions to the acid-covered Si sidewalls. A change in surface tension during BSA film formation then causes the pSi layer to buckle and lift-off the underlying Si substrate. FTIR results from the modified pSi surfaces showed the presence of strong characteristic Amide I, II and III vibrational bands after BSA adsorption.

Nanoparticle albumin-bound (nab-paclitaxel for the treatment of pancreas ductal adenocarcinoma

Directory of Open Access Journals (Sweden)

Narayanan V

2015-01-01

Full Text Available Vignesh Narayanan,1 Colin D Weekes1,2 1Division of Medical Oncology, Department of Medicine, 2Developmental Therapeutics Program, University of Colorado Cancer Center, University of Colorado School of Medicine, Aurora, CO, USA Abstract: Pancreatic adenocarcinoma is a leading cause of cancer-related mortality worldwide, and surgical resection offers the only chance of cure. Since the majority of patients have unresectable disease at presentation, the emphasis has been on identifying effective chemotherapy regimens to prolong survival and control tumor burden. Gemcitabine has been the cornerstone of treatment ever since it was discovered to be an active agent in advanced pancreatic cancer nearly two decades ago, but the overall prognosis in patients with metastatic disease remains dismal. A dense fibrotic stroma around the tumor devoid of vasculature and the resultant hypoxic tumor microenvironment are implicated in the chemotherapy-resistant nature of this malignancy. In recent years, a growing body of literature has further elucidated several aspects of pancreatic tumor biology, such as its ability to utilize albumin from the peritumoral tissues to support its metabolic needs. High-pressure homogenization of paclitaxel with nanoparticle albumin results in the formation of soluble 130 nm complexes with albumin acting as the carrier for the otherwise hydrophobic paclitaxel. Once these complexes reach the tumor milieu, they act by depleting the tumor stroma. In addition, paclitaxel is also transported into the tumor cell along with albumin, where it then exerts its antineoplastic activity. Nanoparticle albumin-bound (nab-paclitaxel also increases gemcitabine levels inside the tumor cells by inhibiting cytidine deaminase, the enzyme that degrades gemcitabine. This review focuses on proposed mechanisms of efficacy of nab-paclitaxel in pancreatic cancer and discusses the preclinical and clinical studies of relevance. Keywords: pancreatic

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...

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

International Nuclear Information System (INIS)

Jalali, Fahimeh; Dorraji, Parisa S.; Mahdiuni, Hamid

2014-01-01

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 (K a ) 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

Spectroscopic study of the interaction of styrylcyanine dyes Sbo, Sil and their derivatives with bovine serum albumin.

Science.gov (United States)

Kurtaliev, Eldar N

2011-07-01

The spectral-luminescent characteristics of newly synthesized styrylcyanine dyes on the base of dyes Sbo ((E)-2-(4-(dimethylamino)styryl)-3-methylbenzo[d]oxazol-3-ium iodide) and Sil ((E)-2-(4-(dimethylamino)styryl)-1,3,3-trimethyl-3H-indolium perchlorate) in aqueous solutions without and in the presence of bovine serum albumin (BSA) were studied. It was established that the absorption spectra of dyes Tol-6, Dbo-10 and Dil-10 with increasing amount of BSA appear new bands with λ(max)=505 nm, λ(max)=512 nm and λ(max)=566 nm, respectively, whose intensity increases in proportion to the amount of albumin. The intensity of the glow of the main band of fluorescence in the presence of BSA sharply increases. The binding constant (K) and the number of binding sites (N) of studied dyes with BSA were determined. The dependence of binding constants with BSA on the dipole moment of dye molecules was determined, which indicates that besides electrostatic forces of attraction between molecules styrylcyanine dyes with BSA, hydrophobic interactions are essential. © Springer Science+Business Media, LLC 2011

Spectroscopic studies of 7, 8-dihydroxy-4-methylcoumarin and its interaction with bovine serum albumin

Energy Technology Data Exchange (ETDEWEB)

Hussein, Belal H.M., E-mail: belalhussein102@yahoo.co [Chemistry Department, Faculty of Science, Suez Canal University, Ismailia 41522 (Egypt)

2011-05-15

The absorption and fluorescence spectra of 7, 8-dihydroxy-4-methylcoumarin (DHMC) in ethanol-water (1:9 v/v) solution at varying pH values were investigated . The interaction between DHMC and bovine serum albumin (BSA) was investigated by fluorescence, FT-IR, and circular dichroism (CD) spectroscopy. The Stern-Volmer quenching constant (K{sub SV}), the quenching rate constant of the bimolecular reaction (K{sub q}), the binding constant, and number of binding sites (n) of DHMC with BSA were evaluated. The results showed that DHMC quenches the fluorescence intensity of BSA through a static quenching process. Positive value of entropy change ({Delta}S) and negative value of enthalpy change ({Delta}H) of the BSA-DHMC interaction were obtained according to the van't Hoff equation. The interaction between DHMC and BSA was driven mainly by hydrophobic forces. The binding process was spontaneous and exothermic. The binding distance between the tryptophan residue in BSA and the DHMC was found to be about 2.6 nm based on the Foerster theory of non-radiation energy transfer. - Research highlights: {yields} 7,8-dihydroxy-4-methylcoumarin (DHMC) quenched the bovine serum albumin (BSA) fluorescence. {yields} The formation of the DHMC-BSA complex was spontaneous through a static quenching process. {yields} The polarity around the tryptophan residues decreased with the increase of DHMC concentration.

Interaction of silicon nanoparticles with the molecules of bovine serum albumin in aqueous solutions

International Nuclear Information System (INIS)

Anenkova, K A; Sergeeva, I A; Petrova, G P; Fedorova, K V; Osminkina, L A; Timoshenko, Viktor Yu

2011-01-01

Using the method of photon-correlation spectroscopy, the coefficient of translational diffusion D t and the hydrodynamic radius R of the particles in aqueous solutions of the bovine serum albumin, containing silicon nanoparticles, are determined. The character of the dependence of these parameters on the concentration of the protein indicates the absence of interaction between the studied particles in the chosen range of albumin concentrations 0.2 - 1.0 mg mL -1 . (optical technologies in biophysics and medicine)

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.

"Smart" nickel oxide based core-shell nanoparticles for combined chemo and photodynamic cancer therapy.

Science.gov (United States)

Bano, Shazia; Nazir, Samina; Munir, Saeeda; AlAjmi, Mohamed Fahad; Afzal, Muhammad; Mazhar, Kehkashan

2016-01-01

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/cm(2), 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.

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.

Fluorescent analysis of interaction of flavonols with hemoglobin and bovine serum albumin

Science.gov (United States)

Sentchouk, V. V.; Bondaryuk, E. V.

2007-09-01

We have studied the fluorescent properties of flavonols (quercetin, fisetin, morin, rutin) with the aim of studying possible interaction with hemoglobin and bovine serum albumin (BSA). We observed an increase in the intensity of intrinsic fluorescence for all the flavonols except rutin in the presence of BSA. From the changes in the fluorescence spectra, we concluded that tautomeric forms are formed on interaction with hemoglobin. We determined the interconnection between the structure of related flavonols and their fluorescent properties on interaction with proteins, and we determined the binding constants for binding with BSA and hemoglobin.

Study of interactions of an anticancer drug neratinib with bovine serum albumin: Spectroscopic and molecular docking approach

Science.gov (United States)

Wani, Tanveer A.; Bakheit, Ahmed H.; Abounassif, M. A.; Zargar, Seema

2018-03-01

Binding of therapeutic agents to plasma proteins, particularly to serum albumin, provides valuable information in the drug development. This study was designed to evaluate the binding interaction of neratinib with bovine serum albumin (BSA). Neratinib blocks HER2 signaling and is effective in trastuzumab-resistant breast cancer treatment. Spectrofluorometric, UV spectrophotometric, and fourier transform infrared (FT-IR) and molecular docking experiments were performed to study this interaction. The fluorescence of BSA is attributed to the presence of tryptophan (Trp) residues. The fluorescence of BSA in presence of neratinib was studied using the excitation wavelength of 280 nm and the emission was measured at 300-500 nm at three different temperatures. Neratinib quenched the BSA intrinsic fluorescence by static mechanism. A complex formation occurred due to the interaction leading to BSA absorption shift. The fluorescence, UV- absorption, three dimensional fluorescence and FT-IR data showed conformational changes occurred in BSA after interaction with neratinib. The binding constant values decreased as the temperature increased suggesting an instable complex formation at high temperature. Site I (sub-domain IIA) was observed as the principal binding site for neratinib. Hydrogen bonding and Van der Waals forces were suggested to be involved in the BSA-neratinib interaction due to the negative values of entropy and enthalpy changes.

Study of Interactions of an Anticancer Drug Neratinib With Bovine Serum Albumin: Spectroscopic and Molecular Docking Approach

Directory of Open Access Journals (Sweden)

Tanveer A. Wani

2018-03-01

Full Text Available Binding of therapeutic agents to plasma proteins, particularly to serum albumin, provides valuable information in the drug development. This study was designed to evaluate the binding interaction of neratinib with bovine serum albumin (BSA. Neratinib blocks HER2 signaling and is effective in trastuzumab-resistant breast cancer treatment. Spectrofluorometric, UV spectrophotometric, and fourier transform infrared (FT-IR and molecular docking experiments were performed to study this interaction. The fluorescence of BSA is attributed to the presence of tryptophan (Trp residues. The fluorescence of BSA in presence of neratinib was studied using the excitation wavelength of 280 nm and the emission was measured at 300-500 nm at three different temperatures. Neratinib quenched the BSA intrinsic fluorescence by static mechanism. A complex formation occurred due to the interaction leading to BSA absorption shift. The fluorescence, UV- absorption, three dimensional fluorescence and FT-IR data showed conformational changes occurred in BSA after interaction with neratinib. The binding constant values decreased as the temperature increased suggesting an instable complex formation at high temperature. Site I (sub-domain IIA was observed as the principal binding site for neratinib. Hydrogen bonding and Van der Waals forces were suggested to be involved in the BSA-neratinib interaction due to the negative values of entropy and enthalpy changes.

Robust one pot synthesis of colloidal silver nanoparticles by simple redox method and absorbance recovered sensing.

Science.gov (United States)

Salman, Muhammad; Iqbal, Mahwish; El Ashry, El Sayed H; Kanwal, Shamsa

2012-01-01

Conventional synthesis of silver nanoparticles employs a reducing agent and a capping agent. In this report water-soluble silver nanoparticles (AgNPs) were prepared facilely by chemical reduction of Ag(I) ions. 4-Amino-3-(d-gluco-pentitol-1-yl)-4,5-dihydro-1,2,4-triazole-5-thione (AGTT) was used both as reducing and stabilizing agent. Direct heating methodology was found to be more suitable for achieving particles with a hydrodynamic diameter of ~20 nm. AGTT exists as tautomer in solution form and our studies indicate that -NH(2) group is involved in the reduction and stabilization of Ag(+) and thione (Δ=S) group of AGTT is possibly involved in stabilizing the nanoparticles via coordinate covalent linkage. Characterization of synthesized silver nanoparticles was performed by UV-vis, FT-IR and by FESEM. Based on the absorption properties of synthesized AgNPs, we used AgNPs to detect bovine serum albumin (BSA) and AgNPs-BSA composite nanoprobe was further applied to detect Cu(2+) based on absorbance recovery. The proposed method has advantages over existing methods in terms of rapid synthesis and stability of AgNPs and their applications. Analysis is reproducible, cost effective and highly sensitive. The lowest detectable concentration of BSA in this approach is 3 nM, and for Cu(2+) it can detect upto 200 pM. Copyright © 2012 Elsevier B.V. All rights reserved.

Albumin nanoparticles targeted with Apo E enter the CNS by transcytosis and are delivered to neurones.

Science.gov (United States)

Zensi, Anja; Begley, David; Pontikis, Charles; Legros, Celine; Mihoreanu, Larisa; Wagner, Sylvia; Büchel, Claudia; von Briesen, Hagen; Kreuter, Jörg

2009-07-01

The blood-brain barrier (BBB) represents a considerable obstacle to brain entry of the majority of drugs and thus severely restricts the therapy of many serious CNS diseases including brain tumours, brain HIV, Alzheimer and other neurodegenerative diseases. The use of nanoparticles coated with polysorbate 80 or with attached apolipoprotein E has enabled the delivery of drugs across the BBB. However, the mechanism of this enhanced transport is still not fully understood. In this present study, human serum albumin nanoparticles, with covalently bound apolipoprotein E (Apo E) as a targetor as well as without apolipoprotein E, were manufactured and injected intravenously into SV 129 mice. The animals were sacrificed after 15 and 30 min, and their brains were examined by transmission electron microscopy. Only the nanoparticles with covalently bound apolipoprotein E were detected in brain capillary endothelial cells and neurones, whereas no uptake into the brain was detectable with nanoparticles without apolipoprotein E. We have also demonstrated uptake of the albumin/ApoE nanoparticles into mouse endothelial (b.End3) cells in vitro and their intracellular localisation. These findings indicate that nanoparticles with covalently bound apolipoprotein E are taken up into the cerebral endothelium by an endocytic mechanism followed by transcytosis into brain parenchyma.

Toxicity of silver nanoparticles in zebrafish models

Energy Technology Data Exchange (ETDEWEB)

Asharani, P V; Valiyaveettil, Suresh [Department of Chemistry, Faculty of Science, National University of Singapore, 3 Science Drive 3, 117543 (Singapore); Wu Yilian; Gong Zhiyuan [Department of Biological Sciences, National University of Singapore, Science Drive 4, 117543 (Singapore)], E-mail: chmsv@nus.edu.sg

2008-06-25

This study was initiated to enhance our insight on the health and environmental impact of silver nanoparticles (Ag-np). Using starch and bovine serum albumin (BSA) as capping agents, silver nanoparticles were synthesized to study their deleterious effects and distribution pattern in zebrafish embryos (Danio rerio). Toxicological endpoints like mortality, hatching, pericardial edema and heart rate were recorded. A concentration-dependent increase in mortality and hatching delay was observed in Ag-np treated embryos. Additionally, nanoparticle treatments resulted in concentration-dependent toxicity, typified by phenotypes that had abnormal body axes, twisted notochord, slow blood flow, pericardial edema and cardiac arrhythmia. Ag{sup +} ions and stabilizing agents showed no significant defects in developing embryos. Transmission electron microscopy (TEM) of the embryos demonstrated that nanoparticles were distributed in the brain, heart, yolk and blood of embryos as evident from the electron-dispersive x-ray analysis (EDS). Furthermore, the acridine orange staining showed an increased apoptosis in Ag-np treated embryos. These results suggest that silver nanoparticles induce a dose-dependent toxicity in embryos, which hinders normal development.

Toxicity of silver nanoparticles in zebrafish models

International Nuclear Information System (INIS)

Asharani, P V; Valiyaveettil, Suresh; Wu Yilian; Gong Zhiyuan

2008-01-01

This study was initiated to enhance our insight on the health and environmental impact of silver nanoparticles (Ag-np). Using starch and bovine serum albumin (BSA) as capping agents, silver nanoparticles were synthesized to study their deleterious effects and distribution pattern in zebrafish embryos (Danio rerio). Toxicological endpoints like mortality, hatching, pericardial edema and heart rate were recorded. A concentration-dependent increase in mortality and hatching delay was observed in Ag-np treated embryos. Additionally, nanoparticle treatments resulted in concentration-dependent toxicity, typified by phenotypes that had abnormal body axes, twisted notochord, slow blood flow, pericardial edema and cardiac arrhythmia. Ag + ions and stabilizing agents showed no significant defects in developing embryos. Transmission electron microscopy (TEM) of the embryos demonstrated that nanoparticles were distributed in the brain, heart, yolk and blood of embryos as evident from the electron-dispersive x-ray analysis (EDS). Furthermore, the acridine orange staining showed an increased apoptosis in Ag-np treated embryos. These results suggest that silver nanoparticles induce a dose-dependent toxicity in embryos, which hinders normal development

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

International Nuclear Information System (INIS)

Naveenraj, Selvaraj; Solomon, Rajadurai Vijay; Venuvanalingam, Ponnambalam; Asiri, Abdullah M.; Anandan, Sambandam

2013-01-01

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

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)

Poór, Miklós; Li, Yin; Matisz, Gergely; Kiss, László; Kunsági-Máté, Sándor; Kőszegi, Tamás

2014-01-01

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

Highly selective BSA imprinted polyacrylamide hydrogels facilitated by a metal-coding MIP approach.

Science.gov (United States)

El-Sharif, H F; Yapati, H; Kalluru, S; Reddy, S M

2015-12-01

We report the fabrication of metal-coded molecularly imprinted polymers (MIPs) using hydrogel-based protein imprinting techniques. A Co(II) complex was prepared using (E)-2-((2 hydrazide-(4-vinylbenzyl)hydrazono)methyl)phenol; along with iron(III) chloroprotoporphyrin (Hemin), vinylferrocene (VFc), zinc(II) protoporphyrin (ZnPP) and protoporphyrin (PP), these complexes were introduced into the MIPs as co-monomers for metal-coding of non-metalloprotein imprints. Results indicate a 66% enhancement for bovine serum albumin (BSA) protein binding capacities (Q, mg/g) via metal-ion/ligand exchange properties within the metal-coded MIPs. Specifically, Co(II)-complex-based MIPs exhibited 92 ± 1% specific binding with Q values of 5.7 ± 0.45 mg BSA/g polymer and imprinting factors (IF) of 14.8 ± 1.9 (MIP/non-imprinted (NIP) control). The selectivity of our Co(II)-coded BSA MIPs were also tested using bovine haemoglobin (BHb), lysozyme (Lyz), and trypsin (Tryp). By evaluating imprinting factors (K), each of the latter proteins was found to have lower affinities in comparison to cognate BSA template. The hydrogels were further characterised by thermal analysis and differential scanning calorimetry (DSC) to assess optimum polymer composition. The development of hydrogel-based molecularly imprinted polymer (HydroMIPs) technology for the memory imprinting of proteins and for protein biosensor development presents many possibilities, including uses in bio-sample clean-up or selective extraction, replacement of biological antibodies in immunoassays and biosensors for medicine and the environment. Biosensors for proteins and viruses are currently expensive to develop because they require the use of expensive antibodies. Because of their biomimicry capabilities (and their potential to act as synthetic antibodies), HydroMIPs potentially offer a route to the development of new low-cost biosensors. Herein, a metal ion-mediated imprinting approach was employed to metal-code our

Selective fluorescence resonance energy transfer from serum albumins to a bio-active 3-pyrazolyl-2-pyrazoline derivative: A spectroscopic analysis

Energy Technology Data Exchange (ETDEWEB)

Sarkar, Arindam [Department of Chemistry, Jadavpur University, Kolkata 700032 (India); Bhattacharya, Subhash Chandra, E-mail: sbjuchem@yahoo.com [Department of Chemistry, Jadavpur University, Kolkata 700032 (India)

2012-10-15

A novel fluorescent probe and pharmaceutically significant: 3-pyrazolyl-2-pyrazoline derivative (PYZ) has been selected as an acceptor molecule for fluorescence resonance energy transfer (FRET) interaction with serum albumins. Steady state and time resolved fluorescence techniques were applied to elucidate the nature of interaction of PYZ with serum albumins (BSA and HSA). Negligible FRET mediated emission occurred in the case of HSA but an efficient FRET mediated emission resulted in case of BSA. To gain further insight into the FRET selectivity of PYZ with the proteins, FRET from L-tryptophan (donor; native tryptophan) to PYZ (acceptor) was performed with the aim of getting an idea about the steric restrictions imposed on PYZ by the other groups present in BSA and HSA. The studies revealed that the surface bound Trp-134 in BSA allows an efficient FRET process with PYZ while the buried Trp-214 in HSA does not. The unusual selectivity for FRET in case of PYZ and the serum albumins has also been attributed to the complex structure of PYZ due to the presence of bulkier phenyl moieties in it. The complex nature of the excited state photophysics of tryptophan (Trp) in proteins also accounts for this FRET selectivity of PYZ with BSA and HSA. - Highlights: Black-Right-Pointing-Pointer FRET from BSA/HSA to PYZ was monitored using steady state and time resolved fluorescence methods. Black-Right-Pointing-Pointer Efficient FRET process resulted in BSA-PYZ system in contrast with the HSA-PYZ system. Black-Right-Pointing-Pointer Surface bound Trp-134 in BSA facilitates the FRET process with PYZ than the buried Trp-214 in HSA. Black-Right-Pointing-Pointer Rigid and complex structure of PYZ also accounts for the FRET selectivity of PYZ with BSA/HSA.

Characterization of the binding of 2-mercaptobenzimidazole to bovine serum albumin.

Science.gov (United States)

Teng, Yue; Zou, Luyi; Huang, Ming; Zong, Wansong

2015-04-01

2-Mercaptobenzimidazole (MBI) is widely utilized as a corrosion inhibitor, copper-plating brightener and rubber accelerator. The residue of MBI in the environment is potentially harmful to human health. In this article, the interaction of MBI with bovine serum albumin (BSA) was explored using spectroscopic and molecular docking methods under physiological conditions. The positively charged MBI can spontaneously bind with the negatively charged BSA through electrostatic forces with one binding site. The site marker competition experiments and the molecular docking study revealed that MBI bound into site II (subdomain IIIA) of BSA, which further led to some secondary structure and microenvironmental changes of BSA. This work provides useful information on understanding the toxicological actions of MBI at the molecular level. Copyright © 2015 John Wiley & Sons, Ltd.

Probing the interaction of a new synthesized CdTe quantum dots with human serum albumin and bovine serum albumin by spectroscopic methods

Energy Technology Data Exchange (ETDEWEB)

Bardajee, Ghasem Rezanejade, E-mail: rezanejad@pnu.ac.ir; 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 (ΔG < 0, ΔH < 0 and ΔS < 0) were indicated that binding reaction was spontaneous and van der Waals interactions and hydrogen-bond interactions played a major role in stabilizing the CdTe-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. - Highlights: • The CdTe quantum dots coated with polyacrylamide grafted onto sodium alginate. • The

The novel albumin-chitosan core-shell nanoparticles for gene delivery: preparation, optimization and cell uptake investigation

Energy Technology Data Exchange (ETDEWEB)

Karimi, Mahdi [Tarbiat Modares University, Department of Nanobiotechnology, Faculty of Biological Sciences (Iran, Islamic Republic of); Avci, Pinar [Massachusetts General Hospital, Wellman Center for Photomedicine (United States); Mobasseri, Rezvan [Tarbiat Modares University, Department of Nanobiotechnology, Faculty of Biological Sciences (Iran, Islamic Republic of); Hamblin, Michael R. [Massachusetts General Hospital, Wellman Center for Photomedicine (United States); Naderi-Manesh, Hossein, E-mail: naderman@modares.ac.ir [Tarbiat Modares University, Department of Nanobiotechnology, Faculty of Biological Sciences (Iran, Islamic Republic of)

2013-05-15

Natural polymers and proteins such as chitosan (CS) and albumin (Alb) have recently attracted much attention both in drug delivery and gene delivery. The underlying rationale is their unique properties such as biodegradability, biocompatibility and controlled release. This study aimed to prepare novel albumin-chitosan-DNA (Alb-CS-DNA) core-shell nanoparticles as a plasmid delivery system and find the best conditions for their preparation. Phase separation method and ionic interaction were used for preparation of Alb nanoparticles and Alb-CS-DNA core-shell nanoparticles, respectively. The effects of three important independent variables (1) CS/Alb mass ratio, (2) the ratios of moles of the amine groups of cationic polymers to those of the phosphate groups of DNA (N/P ratio), and (3) Alb concentration, on the nanoparticle size and loading efficiency of the plasmid were investigated and optimized through Box-Behnken design of response surface methodology (RSM). The optimum conditions were found to be CS/Alb mass ratio = 3, N/P ratio = 8.24 and Alb concentration = 0.1 mg/mL. The most critical factors for the size of nanoparticles and loading efficiency were Alb concentration and N/P ratio. The optimized nanoparticles had an average size of 176 {+-} 3.4 nm and loading efficiency of 80 {+-} 3.9 %. Cytotoxicity experiments demonstrated that the prepared nanoparticles were not toxic. The high cellular uptake of nanoparticles ({approx}85 %) was shown by flow cytometry and fluorescent microscopy.

Assessing protein oxidation by inorganic nanoparticles with enzyme-linked immunosorbent assay (ELISA).

Science.gov (United States)

Sun, Wenjie; Luna-Velasco, Antonia; Sierra-Alvarez, Reyes; Field, Jim A

2013-03-01

Growth in the nanotechnology industry is leading to increased production of engineered nanoparticles (NPs). This has given rise to concerns about the potential adverse and toxic effects to biological system and the environment. An important mechanism of NP toxicity is oxidative stress caused by the formation of reactive oxygen species (ROS) or via direct oxidation of biomolecules. In this study, a protein oxidation assay was developed as an indicator of biomolecule oxidation by NPs. The oxidation of the protein, bovine serum albumin (BSA) was evaluated with an enzyme-linked immunosorbent assay (ELISA) to measure the protein carbonyl derivatives formed from protein oxidation. The results showed that some NPs such as Cu(0), CuO, Mn(2)O(3), and Fe(0) caused oxidation of BSA; whereas, many of the other NPs tested were not reactive or very slowly reactive with BSA. The mechanisms involved in the oxidation of BSA protein by the reactive NPs could be attributed to the combined effects of ROS-dependent and direct protein oxidation mechanisms. The ELISA assay is a promising method for the assessment of protein oxidation by NPs, which can provide insights on NP toxicity mechanisms. Copyright © 2012 Wiley Periodicals, Inc.

Protections of bovine serum albumin protein from damage on functionalized graphene-based electrodes by flavonoids

Energy Technology Data Exchange (ETDEWEB)

Sun, Bolu [School of Pharmacy, Lanzhou University, Lanzhou 730000 (China); Gou, Yuqiang [Lanzhou Military Command Center for Disease Prevention and Control, Lanzhou 730000 (China); Xue, Zhiyuan; Zheng, Xiaoping; Ma, Yuling [School of Pharmacy, Lanzhou University, Lanzhou 730000 (China); Hu, Fangdi, E-mail: hufd@lzu.edu.cn [School of Pharmacy, Lanzhou University, Lanzhou 730000 (China); Zhao, Wanghong, E-mail: wanghongzhao@sina.com [Department of Stomatology, Nanfang Hospital, Southern Medical University, Guangzhou 51515 (China)

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 40 min incubation time and in the pH 5.0 Fenton reagent system (12.5 mM FeSO{sub 4}, 50 mM H{sub 2}O{sub 2}). 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){sub 3}{sup 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. - Highlights: • Hydroxyl radicals were produced by Fenton reagents. • An electrochemical bovine serum albumin (BSA) damage sensor was successfully fabricated. • The proposed biosensor can assess the antioxidant capacity of four flavonoids. • The order of antioxidant

Protections of bovine serum albumin protein from damage on functionalized graphene-based electrodes by flavonoids

International Nuclear Information System (INIS)

Sun, Bolu; Gou, Yuqiang; Xue, Zhiyuan; Zheng, Xiaoping; Ma, Yuling; Hu, Fangdi; Zhao, Wanghong

2016-01-01

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 40 min incubation time and in the pH 5.0 Fenton reagent system (12.5 mM FeSO_4, 50 mM H_2O_2). 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. - Highlights: • Hydroxyl radicals were produced by Fenton reagents. • An electrochemical bovine serum albumin (BSA) damage sensor was successfully fabricated. • The proposed biosensor can assess the antioxidant capacity of four flavonoids. • The order of antioxidant activities of flavonoids is

Study of the interaction between mercury (II) and bovine serum albumin by spectroscopic methods.

Science.gov (United States)

Chunmei, Dai; Cunwei, Ji; Huixiang, Lan; Yuze, Song; Wei, Yang; Dan, Zheng

2014-03-01

Mercury is a significant environmental pollutant that originates from industry. Mercury will bind with albumin and destroy biological functions in humans if it enters the blood. In this paper, the interaction between mercury (II) and bovine serum albumin (BSA) was investigated in vitro by fluorescence, UV-Vis absorption and circular dichroism (CD) under simulated physiological conditions. This study proves that the probable quenching mechanism of BSA by mercury (II) was mainly static quenching due to the formation of a mercury (II)-BSA complex. The quenching constant K(a) and the corresponding thermodynamic parameters (ΔH, ΔS and ΔG) at four different temperatures were calculated by a modified Stern-Volmer equation and the van't Hoff equation, respectively. The results revealed that the interaction between mercury (II) and BSA was mainly enthalpy-driven and that hydrogen bonding and van der Waals forces played a major role in the reaction. The obtained data for binding sites of n approximately equal to 1 indicated that there was a single class of binding site for the BSA with mercury (II). The value of the distance r (3.55 nm), determined by Föster's non-radioactive energy transfer theory, suggested that the energy transfer from BSA to mercury (II) occurred with a high probability. The conformational investigation from synchronous fluorescence, CD spectroscopy and three-dimensional fluorescence showed that the presence of mercury (II) resulted in micro-environmental and conformational changes of the BSA molecules, which may be responsible for the toxicity of mercury (II) in vivo. Copyright © 2014 Elsevier B.V. All rights reserved.

"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

Colorimetric detection of Cr (VI) based on the leaching of gold nanoparticles using a paper-based sensor.

Science.gov (United States)

Guo, Jian-Feng; Huo, Dan-Qun; Yang, Mei; Hou, Chang-Jun; Li, Jun-Jie; Fa, Huan-Bao; Luo, Hui-Bo; Yang, Ping

2016-12-01

Herein, we have developed a simple, sensitive and paper-based colorimetric sensor for the selective detection of Chromium (Ⅵ) ions (Cr (VI)). Silanization-titanium dioxide modified filter paper (STCP) was used to trap bovine serum albumin capped gold nanoparticles (BSA-Au NPs), leading to the fabrication of BSA-Au NPs decorated membrane (BSA-Au NPs/STCP). The BSA-Au NPs/STCP operated on the principle that BSA-Au NPs anchored on the STCP were gradually etched by Cr (VI) as the leaching process of gold in the presence of hydrobromic acid (HBr) and hence induced a visible color change. Under optimum conditions, the paper-based colorimetric sensor showed clear color change after reaction with Cr (VI) as well as with favorable selectivity to a variety of possible interfering counterparts. The amount-dependent colorimetric response was linearly correlated with the Cr (VI) concentrations ranging from 0.5µM to 50.0µM with a detection limit down to 280nM. Moreover, the developed cost-effective colorimetric sensor has been successfully applied to real environmental samples which demonstrated the potential for field applications. Copyright © 2016 Elsevier B.V. All rights reserved.

A centrifugation-based physicochemical characterization method for the interaction between proteins and nanoparticles

Science.gov (United States)

Bekdemir, Ahmet; Stellacci, Francesco

2016-10-01

Nanomedicine requires in-depth knowledge of nanoparticle-protein interactions. These interactions are studied with methods limited to large or fluorescently labelled nanoparticles as they rely on scattering or fluorescence-correlation signals. Here, we have developed a method based on analytical ultracentrifugation (AUC) as an absorbance-based, label-free tool to determine dissociation constants (KD), stoichiometry (Nmax), and Hill coefficient (n), for the association of bovine serum albumin (BSA) with gold nanoparticles. Absorption at 520 nm in AUC renders the measurements insensitive to unbound and aggregated proteins. Measurements remain accurate and do not become more challenging for small (sub-10 nm) nanoparticles. In AUC, frictional ratio analysis allows for the qualitative assessment of the shape of the analyte. Data suggests that small-nanoparticles/protein complexes significantly deviate from a spherical shape even at maximum coverage. We believe that this method could become one of the established approaches for the characterization of the interaction of (small) nanoparticles with proteins.

Investigation of the binding affinity in vitamin B12-Bovine serum albumin system using various spectroscopic methods

Science.gov (United States)

Makarska-Bialokoz, Magdalena

2017-09-01

The binding affinity between vitamin B12 (VitB12) and bovine serum albumin (BSA) has been investigated in aqueous solution at pH = 7.4, employing UV-vis absorption and steady-state, synchronous and three-dimensional fluorescence spectra techniques. Representative effects noted for BSA intrinsic fluorescence resulting from the interactions with VitB12 confirm the formation of π-π stacked non-covalent and non-fluorescent complexes in the system VitB12-BSA. All the determined parameters, the binding, fluorescence quenching and bimolecular quenching rate constants (of the order of 104 L mol- 1, 103 L mol- 1 and 1011 L mol- 1 s- 1, respectively), as well as Förster resonance energy transfer parameters validate the mechanism of static quenching. The interaction with VitB12 induces folding of the polypeptide chains around Trp residues of BSA, resulting in a more hydrophobic surrounding. Presented outcomes suggest that the addition of VitB12 can lead to the more organized BSA conformation and its more folded tertiary structure, what could influence the physiological functions of bovine serum albumin, notably in case of its overuse or abnormal metabolism.

Pengaruh penggantian Bovine Serum Albumin (BSA dengan putih telur pada pengencer CEP-2 terhadap kualitas semen sapi Peranakan Ongole pada suhu penyimpanan 3-5oC

Directory of Open Access Journals (Sweden)

Nisa’us Sholikah

2016-04-01

Full Text Available Purpose of this research was to investigate the effect of Bovine Serum Albumin substitution by albumen on CEP-2 to semen quality Ongole CrossBred bull stored at 3-5oC. Research was conducted at Research Centre Beef Cattle Laboratory, Grati, Pasuruan on February 2016. Semen diluent was divided into two groups, there were P0 (90% CEP-2 + 10% Egg Yolk (EY; and P1 (90% CEP + 0.4% albumen + 10% EY. Data of the research were analyzed using paired design t test. The result showed that after eight days chilled preservation, percentage of motility P1 (47.4±10.9% was higher than P0 (47±9.2%. Percentage of viability P0 (83.1±1.9% was higher than P1 (81.3±1.5%. Percentage of abnormality P1 (3.6±0.4% was lower than P0 (3.8±0.3%. Total motile sperm count after six days chilled preservation was significantly higher in all treatments compared to the standard criteria of SNI 40% motile sperm/ml. The conclusion of this research was 0,4% albumen could replace the BSA capability on CEP-2. Keywords: CEP-2, Bovine Serum Albumin, chilled preservation, semen quality

Cryo-electron tomography investigation of serum albumin-camouflaged tobacco mosaic virus nanoparticles.

Science.gov (United States)

Gulati, Neetu M; Pitek, Andrzej S; Steinmetz, Nicole F; Stewart, Phoebe L

2017-03-09

Nanoparticles offer great potential in drug delivery and imaging, but shielding strategies are necessary to increase circulation time and performance. Structure-function studies are required to define the design rules to achieve effective shielding. With several formulations reaching clinical testing and approval, the ability to assess and detail nanoparticle formulations at the single particle level is becoming increasingly important. To address this need, we use cryo-electron tomography (cryo-ET) to investigate stealth-coated nanoparticles. As a model system, we studied the soft matter nanotubes formed by tobacco mosaic virus (TMV) coated with human serum albumin (SA) stealth proteins. Cryo-ET and subtomogram averaging allow for visualization of individual SA molecules and determination of their orientations relative to the TMV surface, and also for measurement of the surface coverage provided by added stealth proteins. This information fills a critical gap in the understanding of the structural morphology of stealth-coated nanoparticles, and therefore cryo-ET may play an important role in guiding the development of future nanoparticle-based therapeutics.

Albumin nanoparticles for glutathione-responsive release of cisplatin: New opportunities for medulloblastoma.

Science.gov (United States)

Catanzaro, Giuseppina; Curcio, Manuela; Cirillo, Giuseppe; Spizzirri, Umile Gianfranco; Besharat, Zein Mersini; Abballe, Luana; Vacca, Alessandra; Iemma, Francesca; Picci, Nevio; Ferretti, Elisabetta

2017-01-30

Redox-responsive nanoparticles were synthesized by desolvation of bovine serum albumin followed by disulfide-bond crosslinking with N, N'-Bis (acryloyl) cystamine. Dynamic light scattering and transmission electron microscopy studies revealed spherical nanoparticles (mean diameter: 83nm, polydispersity index: 0.3) that were glutathione-responsive. Confocal microscopy revealed rapid, efficient internalization of the nanoparticles by Daoy medulloblastoma cells and healthy controls (HaCaT keratinocytes). Cisplatin-loaded nanoparticles with drug:carrier ratios of 5%, 10%, and 20% were tested in both cell lines. The formulation with the highest drug:carrier ratio reduced Daoy and HaCaT cell viability with IC 50 values of 6.19 and 11.17μgmL -1 , respectively. The differential cytotoxicity reflects the cancer cells' higher glutathione content, which triggers more extensive disruption of the disulfide bond-mediated intra-particle cross-links, decreasing particle stability and increasing their cisplatin release. These findings support continuing efforts to improve the safety and efficacy of antineoplastic drug therapy for pediatric brain tumors using selective nanoparticle-based drug delivery systems. Copyright © 2016 Elsevier B.V. All rights reserved.

Self-colored nanoparticles containing naphthalene-bisimide derivatives: Synthesis and protein adsorption study

Energy Technology Data Exchange (ETDEWEB)

Polpanich, Duangporn, E-mail: duangporn@nanotec.or.th [National Nanotechnology Center, National Science and Technology Development Agency, Thailand Science Park, Pathumthani 12120 (Thailand); Asawapirom, Udom; Thiramanas, Raweewan; Piyakulawat, Phimwipha [National Nanotechnology Center, National Science and Technology Development Agency, Thailand Science Park, Pathumthani 12120 (Thailand)

2011-09-15

Highlights: {yields} Novel polymerizable naphthalene-bisimide dyes were designed and synthesized. {yields} Highly monodispersed self-colored nanoparticles were successfully prepared. {yields} Good colloidal stability of the nanoparticles was achieved after protein adsorption. - Abstract: An approach to covalently bound the novel polymerizable dyes, 2,3,6,7-tetrathienyl-1,4,5,8-naphthalenetetracarboxylic-N,N' -di(2-methylallyl)-bisimide (ALN4T) and 2,3,6,7-tetra(2,2'-bithiophene)-1,4,5,8-naphthalenetetracarboxylic-N,N' -di(2-methylallyl)-bisimide (ALN8T), and vinyl monomers for tailoring the self-colored nanoparticles (NPs) was demonstrated. Using the miniemulsion polymerization technique, the NPs with high conversion were synthesized. Examining the particles by scanning electron micrograph (SEM) revealed a uniform size distribution. UV/vis spectroscopy results showed that the colored NPs comprising of ALN4T exhibited the same absorption maxima compared to that of the parent dye, while a hypsochromic shift was observed when using ALN8T. By using bovine serum albumin (BSA) as a model, the amount of protein adsorption ({Gamma}{sub ads}) onto the surface of the colored NPs was evaluated. The {Gamma}{sub ads} on the colored NPs was found to be dictated by synergistic effects of the conformation change of BSA at a given pH and the electrostatic interaction between the protein and the particle surface. The good colloidal stability of the NPs after BSA adsorption was observed by zeta potential measurement. Therefore, the prepared self-colored NPs have potential application in biomedical areas.

Spectroscopic studies on the binding of barbital to bovine serum albumin

International Nuclear Information System (INIS)

Ding Fei; Pan Hong; Li Zhiyuan; Liu Feng; Sun Ying

2009-01-01

In this paper, the interaction between barbital and bovine serum albumin (BSA) was investigated by the method of fluorescence spectroscopy under simulative physiological conditions. Fluorescence data revealed that the fluorescence quenching of BSA by barbital was the result of the formation of BSA-barbital complex, and the effective quenching constants (K a ) were 1.468x10 4 , 1.445x10 4 and 1.403x10 4 M -1 at 297, 303 and 310 K, respectively. The thermodynamic parameters enthalpy change (ΔH) and entropy change (ΔS) for the reaction were calculated to be -2.679 kJ mol -1 and 70.76 J mol -1 K -1 , respectively, according to the van't Hoff equation. The results indicated that hydrophobic and electrostatic interactions were the dominant intermolecular force in stabilizing the complex. The results of synchronous fluorescence spectra showed that binding of barbital with BSA can induce conformational changes in BSA. In addition, the effects of Cu 2+ and Zn 2+ on the constants of BSA-barbital complex were also discussed.

Evaluation on the toxicity of nanoAg to bovine serum albumin

Energy Technology Data Exchange (ETDEWEB)

Liu Rutao, E-mail: rutaoliu@sdu.edu.cn [School of Environmental Science and Engineering, Shandong University, 27 Shanda South Road, Jinan 250100 (China); Sun Feng; Zhang Lijun; Zong Wansong; Zhao Xingchen; Wang Li; Wu Ruolin [School of Environmental Science and Engineering, Shandong University, 27 Shanda South Road, Jinan 250100 (China); Hao Xiaopeng [State Key Laboratory of Crystal Materials, Shandong University, Jinan, 250100 (China)

2009-06-15

Measuring protein damage by nanomaterials may give insight into the mechanisms of toxicity of nanomaterials. The toxic effects of nanoAg on bovine serum albumin (BSA) were thoroughly studied using fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy, resonance light scattering spectroscopy (RLS), circular dichroism spectroscopy (CD) and transmission electron microscopy (TEM). NanoAg had obvious toxic effects on BSA: nanoAg could increase the amount of helix and decrease the beta sheet structure, leading to a loosening of the protein skeleton. In the loose structure, internal hydrophobic amino acids are exposed and the characteristic fluorescence of BSA is obviously quenched. When the ratio of nanoAg and BSA increased to 1: 96 (wt/wt), the impact of nanoAg on the spectral properties leveled off. The RLS spectrum, TEM, CD spectra and electrophoresis results showed that BSA had destroyed the double-layer structure of nanoAg and covered its surface, generating a BSA-nanoAg complex held together by van der Waals and electrostatic forces. This paper provides a new perspective and method for determining the toxic effects of nanoAg on biological macromolecules.

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

Science.gov (United States)

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

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 the interaction. Moreover, the efficiency of energy transfer, and the distance between BSA and acceptor eupatorin, were calculated. The effects of eupatorin on the BSA conformation were analyzed using UV-vis, CD, and synchronous fluorescence. Finally, the binding of eupatorin to BSA was modeled using the molecular docking method. PMID:23839090

Unveiling the stimulatory effects of tartrazine on human and bovine serum albumin fibrillogenesis: Spectroscopic and microscopic study

Science.gov (United States)

Al-Shabib, Nasser Abdulatif; Khan, Javed Masood; Alsenaidy, Mohammad A.; Alsenaidy, Abdulrahman M.; Khan, Mohd Shahnawaz; Husain, Fohad Mabood; Khan, Mohammad Rashid; Naseem, Mohammad; Sen, Priyankar; Alam, Parvez; Khan, Rizwan Hasan

2018-02-01

Amyloid fibrils are playing key role in the pathogenesis of various neurodegenerative diseases. Generally anionic molecules are known to induce amyloid fibril in several proteins. In this work, we have studied the effect of anionic food additive dye i.e., tartrazine (TZ) on the amyloid fibril formation of human serum albumins (HSA) and bovine serum albumin (BSA) at pHs 7.4 and 3.5. We have employed various biophysical methods like, turbidity measurements, Rayleigh Light Scattering (RLS), Dynamic Light Scattering (DLS), intrinsic fluorescence, Congo red assay, far-UV CD, transmission electron microscopy (TEM) and atomic force microscopy (AFM) to decipher the mechanism of TZ-induce amyloid fibril formation in both the serum albumins at pHs 7.4 and 3.5. The obtained results suggest that both the albumins forms amyloid-like aggregates in the presence of 1.0 to 15.0 mM of TZ at pH 3.5, but no amyloid fibril were seen at pH 7.4. The possible cause of TZ-induced amyloid fibril formation is electrostatic and hydrophobic interaction because sulfate group of TZ may have interacted electrostatically with positively charged amino acids of the albumins at pH 3.5 and increased protein-protein and protein-TZ interactions leading to amyloid fibril formation. The TEM, RLS and DLS results are suggesting that BSA forms bigger size amyloids compared to HSA, may be due to high surface hydrophobicity of BSA.

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

Energy Technology Data Exchange (ETDEWEB)

Poór, Miklós [Institute of Laboratory Medicine, University of Pécs, Ifjúság u. 13, Pécs H-7624 (Hungary); Li, Yin; Matisz, Gergely [Department of General and Physical Chemistry, University of Pécs, Pécs H-7624 (Hungary); János Szentágothai Research Center, Pécs H-7624 (Hungary); Kiss, László [Department of General and Physical Chemistry, University of Pécs, Pécs H-7624 (Hungary); Kunsági-Máté, Sándor [Department of General and Physical Chemistry, University of Pécs, Pécs H-7624 (Hungary); János Szentágothai Research Center, Pécs H-7624 (Hungary); Kőszegi, Tamás, E-mail: koszegit@freemail.hu [Institute of Laboratory Medicine, University of Pécs, Ifjúság u. 13, Pécs H-7624 (Hungary)

2014-01-15

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.

Optical, structural and thermodynamic properties of the interaction between tradimefon and serum albumin

Science.gov (United States)

Zhang, Hua-xin; Mei, Ping; Yang, Xi-xiong

2009-04-01

The biological toxicity of a chloric pesticide, tradimefon to bovine serum albumin (BSA) were studied by fluorescence and absorption spectroscopy. The fluorescence quenching mechanism analysis indicates the quenching of BSA by TDF was caused by BSA-TDF complex formation and electrostatic interaction played major role in the reaction. The number of binding sites n and observed binding constant Kb was measured by fluorescence quenching method. The thermodynamic parameters Δ Hθ, Δ Gθ, Δ Sθ at different temperatures were calculated, and the distance r between donor (BSA) and acceptor (TDF) was obtained according to Förster theory of non-radiation energy transfer. Three-dimensional fluorescence spectra, circular dichroism (CD) spectra and synchronous fluorescence spectra were used to investigate the structural change of BSA molecules with addition of TDF and the mechanism of binding reaction was analyzed at molecular level.

Electrochemical Studies of Camptothecin and Its Interaction with Human Serum Albumin

OpenAIRE

Zhao, Jing; Zheng, Xiaofeng; Xing, Wei; Huang, Junyi; Li, Genxi

2007-01-01

Camptothecin, an anticancer component from Camptotheca acuminate, may interact with human serum albumin (HSA) at the subdomain IIA (site I), and then convert to its inactive form(carboxylate form). In this paper, the detailed electrochemical behaviors of camptothecin at a pyrolytic graphite electrode is presented. The interaction between camptothecin and HSA is also studied by electrochemical technique. By comparing with bovine serum albumin (BSA), which is highly homologous to HSA, we prove ...

Investigation of the interaction between trazodone hydrochloride and bovine serum albumin

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Ashoka, S. [Department of Chemistry, Karnatak University, Dharwad-580 003 (India); Seetharamappa, J. [Department of Chemistry, Karnatak University, Dharwad-580 003 (India)]. E-mail: jseetharam@yahoo.com; Kandagal, P.B. [Department of Chemistry, Karnatak University, Dharwad-580 003 (India); Shaikh, S.M.T. [Department of Chemistry, Karnatak University, Dharwad-580 003 (India)

2006-11-15

In this paper, the binding of trazodone hydrochloride (TZH) to bovine serum albumin (BSA) was investigated by spectroscopic (fluorescence, spectrophotometry and circular dichroism) techniques under simulative physiological conditions. A strong fluorescence quenching reaction of TZH to BSA was observed and the quenching mechanism was suggested as dynamic quenching according to the Stern-Volmer equation. The binding constants of TZH with BSA at 288, 302 and 309 K were calculated as (1.56{+-}0.003)x10{sup 4}, (2.31{+-}0.002)x10{sup 4} and (5.44{+-}0.004)x10{sup 4} M{sup -1}, respectively. The thermodynamic parameters, {delta}H {sup 0} and {delta}S {sup 0} were obtained to be 39.86{+-}0.008 kJ mol{sup -1} and 217.89{+-}0.011 J mol{sup -1} K{sup -1}, respectively, which indicated the presence of hydrophobic forces between TZH and BSA. The spectral results observed showed that the binding of TZH to BSA induced conformational changes in BSA. Based on the Foerster's theory of non-radiation energy transfer, the binding average distance, r between donor (BSA) and acceptor (TZH) was found to be 2.4 nm. The effect of common ions on binding of TZH to BSA was also examined.

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

Improvement of interaction between PVA and chitosan via magnetite nanoparticles for drug delivery application.

Science.gov (United States)

Shagholani, Hamidreza; Ghoreishi, Sayed Mehdi; Mousazadeh, Mohammad

2015-01-01

Magnetite nanoparticles were synthesized by coprecipitation under ultrasonication followed by coating with chitosan. Polyvinyl alcohol (PVA) is then combined with the chitosan that coated the magnetite nanoparticles. The combination occurs by hydrogen binding and ionic cross-linking of the amino and hydroxyl groups of chitosan and PVA respectively. The magnetite nanoparticles have an average size of 10.62 nm that was confirmed by TEM. The VSM measurements showed that nanoparticles were superparamagnetic. The coatings on the core nanoparticles were estimated by AAS and the attachments of coating to the nanoparticles were confirmed by FT-IR analysis. Physicochemical properties of nanoparticles were measured by DLS and zeta potential. Naked magnetite, chitosan and PVA coating have zeta potential of +36.4, +48.1 and -12.5 mV respectively. The unspecific adsorption and interaction between nanoparticles and bovine serum albumin (BSA) were investigated systematically by UV-vis spectroscopy method. The nanoparticles that were modified by PVA present low protein adsorption, which makes them a practical choice for preventing opsonization in clinical application and drug delivery. Copyright © 2015. Published by Elsevier B.V.

Up-converter nanophosphor Y2O2S:Er,Yb aminofunctionalized containing or not spherical silica conjugated with BSA

International Nuclear Information System (INIS)

Gelamos, Joao Paulo; Laranja, Marlon Larry; Alvino, Karla Cristina Lombardi; Camacho, Sabrina Alessio; Pires, Ana Maria

2009-01-01

This work reports on the study of the nanophosphor Y 2 O 2 S:Er(2%),Yb(1%) obtained from polymeric resin to be evaluated as fluorescent label with suitable features to conjugate with bio-molecules for bioassay up-converting phosphor technology (UPT) application. A conjugation protocol between bovine serum albumin (BSA) and the aminofunctionalized nanophosphor containing or not spherical silica was established. UV-vis results indicated an effective conjugation between nanophosphor particles and the protein. Up-conversion measurements under 980 nm excitation performed for samples before and after aminofunctionalization showed that nanophosphor particles luminescence features keep unchanged in all cases. All results suggest that the adapted protocol is feasible to provide a nanoparticle-protein effective conjugation preserving nanophosphor optical features. The presence of spherical silica can be considered advantageous to increase conjugation efficiency. Therefore, the developed procedure is applicable for future conjugations between the chosen nanophosphor and the streptavidin protein that takes part in the well known self-recognition system avidin-biotin.

An insight into the optical properties of CdSe quantum dots during their growth in bovine serum albumin solution

International Nuclear Information System (INIS)

Singh, Avinash; Ahmed, M.; Guleria, A.; Singh, A.K.; Adhikari, S.; Rath, M.C.

2016-01-01

Bovine serum albumin (BSA) assisted synthesis of cadmium selenide (CdSe) quantum dots (QDs) exhibits remarkable changes in the optical properties of the QDs as well as BSA during their growth. The growth of these QDs was investigated by recording the UV–visible absorption spectra and room temperature steady state fluorescence at different time intervals after the mixing of the precursors. The growth of these QDs was associated with a quenching of the fluorescence from BSA. The fluorescence from these QDs was found to be associated with several features: (1) a gradual red-shift in its peak position, (2) increase in intensity with an isoemissive point up to few minutes from the time of mixing of the two precursors, and (3) subsequent decrease in intensity reaching a minimum value, which remains almost unchanged thereafter. The decrease and increase in the fluorescence from BSA and CdSe QDs, respectively have been explained on the basis of Förster resonance energy transfer (FRET) as well as the simultaneous growth of these QDs. - Highlights: • CdSe quantum dots were synthesized in the presence of bovine serum albumin (BSA). • Fluorescence from BSA was quenched by during the growth of CdSe quantum dots. • There was an energy transfer from BSA to CdSe quantum dots during their growth. • The emission from CdSe quantum dots was associated with a red-shift.

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.

Binding of carvedilol to serum albumins investigated by multi-spectroscopic and molecular modeling methods

Energy Technology Data Exchange (ETDEWEB)

Safarnejad, Azam; Shaghaghi, Masoomeh [Department of Chemistry, Payame Noor University, P.O. Box. 19395-3697, Tehran (Iran, Islamic Republic of); Dehghan, Golamreza [Department of Biology, Faculty of Natural Sciences, University of Tabriz, Tabriz (Iran, Islamic Republic of); Soltani, Somaieh, E-mail: soltanisomaieh@gmail.com [Drug applied research center and pharmacy faculty, Tabriz University of Medical Sciences, Tabriz (Iran, Islamic Republic of)

2016-08-15

Carvedilol (CAR) binding to human and bovine serum albumins (HSA and BSA) was studied using fluorescence, UV–vis absorption and Fourier transform infrared spectroscopy (FTIR) and molecular docking techniques at different temperatures (288, 298 and 308 K) under physiologic pH. Results obtained from fluorescence data indicated that values of binding sites (n), effective quenching constants (Ka) and binding constants (K{sub b}) decreased under higher temperature and that the quenching mechanism was static. The thermodynamic parameters including enthalpy (ΔH), entropy (ΔS) and Gibb's free energy (ΔG) changes were calculated by the van't Hoff equation and these data showed that hydrogen bonds and Van der Waals contacts were the main binding force in HSA–CAR and BSA–CAR systems. Binding distance (r) between HSA–CAR and BSA–CAR were calculated by the Förster (fluorescence resonance energy transfer (FRET)) method. FTIR absorption studies showed that the secondary structure was changed according to the interaction of HSA/BSA and CAR. Results determined by molecular docking were in agreement with thermodynamic and FRET data and confirmed that the binding mechanism of Carvedilol to HSA and BSA is different. - Highlights: • The quenching mechanism between Carvedilol and HSA /BSA is a static process. • Hydrogen bonds and Van der Waals contacts were stabilized the Carvedilol albumin complexes. • Molecular modeling simulations confirmed the fluorescence spectroscopy and FRET analysis. • According to the binding mechanism differences between HSA and BSA, the results of BSA experiments could not be applied for HSA binding.

Interaction of singlet oxygen with bovine serum albumin and the role of the protein nano-compartmentalization.

Science.gov (United States)

Giménez, Rodrigo E; Vargová, Veronika; Rey, Valentina; Turbay, M Beatriz Espeche; Abatedaga, Inés; Morán Vieyra, Faustino E; Paz Zanini, Verónica I; Mecchia Ortiz, Juan H; Katz, Néstor E; Ostatná, Veronika; Borsarelli, Claudio D

2016-05-01

Singlet molecular oxygen ((1)O2) contributes to protein damage triggering biophysical and biochemical changes that can be related with aging and oxidative stress. Serum albumins, such as bovine serum albumin (BSA), are abundant proteins in blood plasma with different biological functions. This paper presents a kinetic and spectroscopic study of the (1)O2-mediated oxidation of BSA using the tris(2,2'-bipyridine)ruthenium(II) cation [Ru(bpy)3](2+) as sensitizer. BSA quenches efficiently (1)O2 with a total (chemical+physical interaction) rate constant kt(BSA)=7.3(±0.4)×10(8)M(-1)s(-1), where the chemical pathway represented 37% of the interaction. This efficient quenching by BSA indicates the participation of several reactive residues. MALDI-TOF MS analysis of intact BSA confirmed that after oxidation by (1)O2, the mass protein increased the equivalent of 13 oxygen atoms. Time-resolved emission spectra analysis of BSA established that Trp residues were oxidized to N'-formylkynurenine, being the solvent-accessible W134 preferentially oxidized by (1)O2 as compared with the buried W213. MS confirmed oxidation of at least two Tyr residues to form dihydroxyphenylalanine, with a global reactivity towards (1)O2 six-times lower than for Trp residues. Despite the lack of MS evidences, kinetic and chemical analysis also suggested that residues other than Trp and Tyr, e.g. Met, must react with (1)O2. Modeling of the 3D-structure of BSA indicated that the oxidation pattern involves a random distribution of (1)O2 into BSA; allowing also the interaction of (1)O2 with buried residues by its diffusion from the bulk solvent through interconnected internal hydrophilic and hydrophobic grooves. Copyright © 2016 Elsevier Inc. All rights reserved.

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.

Thermodynamic Study of the Interaction of Bovine Serum Albumin and Amino Acids with Cellulose Nanocrystals

OpenAIRE

Lombardo, Salvatore; Eyley, Sam; Schütz, Christina; Van Gorp, Hans; Rosenfeldt, Sabine; Van den Mooter, Guy; Thielemans, Wim

2017-01-01

The interaction of bovine serum albumin (BSA) with sulfated, carboxylated, and pyridinium-grafted cellulose nanocrystals (CNCs) was studied as a function of the degree of substitution by determining the adsorption isotherm and by directly measuring the thermodynamics of interaction. The adsorption of BSA onto positively charged pyridinium-grafted cellulose nanocrystals followed Langmuirian adsorption with the maximum amount of adsorbed protein increasing linearly with increasing degree of sub...

Prevention of hemodynamic and vascular albumin filtration changes in diabetic rats by aldose reductase inhibitors

International Nuclear Information System (INIS)

Tilton, R.G.; Chang, K.; Pugliese, G.; Eades, D.M.; Province, M.A.; Sherman, W.R.; Kilo, C.; Williamson, J.R.

1989-01-01

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

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.

Interactions between 4-(2-dimethylaminoethyloxy)-N-octadecyl-1,8-naphthalimide and serum albumins: Investigation by spectroscopic approach

Energy Technology Data Exchange (ETDEWEB)

Sun Yang; Wei Song [School of Chemical Engineering, Northwest University, No. 229 Taibai North Road, Xi' an, Shaanxi 710069 (China); Zhao Yingyong [Biomedicine Key Laboratory of Shaanxi Province, Northwest University, No. 229 Taibai North Road, Xi' an, Shaanxi 710069 (China); Hu Xiaoyun, E-mail: hxy3275@nwu.edu.cn [Department of Physics, Northwest University, No. 229 Taibai North Road, Xi' an, Shaanxi 710069 (China); Fan Jun, E-mail: fanjun@nwu.edu.cn [School of Chemical Engineering, Northwest University, No. 229 Taibai North Road, Xi' an, Shaanxi 710069 (China)

2012-04-15

A novel 4-(2-dimethylaminoethyloxy)-N-octadecyl-1,8-naphthalimide (DON) has been synthesized as a spectrofluorimetric probe for the determination of proteins. Photophysics of DON in different solvents has been delineated in this paper. Progressive redshift with polarity of solvents in emission and absorption spectra hints at intramolecular charge transfer. The interactions of DON with serum albumins (i.e., human serum albumin (HSA) and bovine serum albumin (BSA)) were studied by fluorescence and absorption spectroscopy. Fluorescence data revealed that the quenching of HSA/BSA by DON were static quenching and the DON-HSA/BSA complexes were formed. The binding constant (K{sub b}) for HSA and was found to be 8.44 Multiplication-Sign 10{sup -4} and 60.26 Multiplication-Sign 10{sup -4} M{sup -1} and the number of binding sites (n) were 1.00 and 1.40, respectively. The thermodynamic parameters, {Delta}H and {Delta}S, for the DON-HSA system was calculated to be -14.83 kJ mol{sup -1} and 23.61 J mol{sup -1} K{sup -1}, indicating the hydrogen bonds and hydrophobic interactions were the dominant intermolecular force. {Delta}H and {Delta}S for the binding of DON with BSA was -60.08 kJ mol{sup -1} and -90.7441 mol{sup -1} K{sup -1}, suggesting the hydrogen bonds and van der Waals force played the main role in the interaction. The results of displacement experiments showed that DON bound HSA/BSA occurred at the Trp-214 proximity, located in subdomain IIA of the serum albumin structure (the warfarin binding pocket). The effect of DON on the conformation of HSA was also analyzed by synchronous and three-dimensional fluorescence spectra. The fluorescence of DON could be quenched by HSA, based on which, a fluorometric method for the determination of microamount protein using DON in the medium of HCl-Tris buffer solution (pH=7.4) was developed. The linear range of the calibration curves was 0.1-10.0 {mu}M for HSA, 0.1-11.2 {mu}M for BSA and 0.2-9.7 {mu}M for egg albumin (EA). The

Interactions between 4-(2-dimethylaminoethyloxy)-N-octadecyl-1,8-naphthalimide and serum albumins: Investigation by spectroscopic approach

International Nuclear Information System (INIS)

Sun Yang; Wei Song; Zhao Yingyong; Hu Xiaoyun; Fan Jun

2012-01-01

A novel 4-(2-dimethylaminoethyloxy)-N-octadecyl-1,8-naphthalimide (DON) has been synthesized as a spectrofluorimetric probe for the determination of proteins. Photophysics of DON in different solvents has been delineated in this paper. Progressive redshift with polarity of solvents in emission and absorption spectra hints at intramolecular charge transfer. The interactions of DON with serum albumins (i.e., human serum albumin (HSA) and bovine serum albumin (BSA)) were studied by fluorescence and absorption spectroscopy. Fluorescence data revealed that the quenching of HSA/BSA by DON were static quenching and the DON–HSA/BSA complexes were formed. The binding constant (K b ) for HSA and was found to be 8.44×10 −4 and 60.26×10 −4 M −1 and the number of binding sites (n) were 1.00 and 1.40, respectively. The thermodynamic parameters, ΔH and ΔS, for the DON–HSA system was calculated to be −14.83 kJ mol −1 and 23.61 J mol −1 K −1 , indicating the hydrogen bonds and hydrophobic interactions were the dominant intermolecular force. ΔH and ΔS for the binding of DON with BSA was −60.08 kJ mol −1 and −90.7441 mol −1 K −1 , suggesting the hydrogen bonds and van der Waals force played the main role in the interaction. The results of displacement experiments showed that DON bound HSA/BSA occurred at the Trp-214 proximity, located in subdomain IIA of the serum albumin structure (the warfarin binding pocket). The effect of DON on the conformation of HSA was also analyzed by synchronous and three-dimensional fluorescence spectra. The fluorescence of DON could be quenched by HSA, based on which, a fluorometric method for the determination of microamount protein using DON in the medium of HCl−Tris buffer solution (pH=7.4) was developed. The linear range of the calibration curves was 0.1–10.0 μM for HSA, 0.1–11.2 μM for BSA and 0.2–9.7 μM for egg albumin (EA). The detection limit (3σ) for HSA was 1.12×10 −10 M, for BSA it was 0.92×10 �

Visual detection of copper(II) ions in blood samples by controlling the leaching of protein-capped gold nanoparticles.

Science.gov (United States)

Lee, Yen-Fei; Deng, Ting-Wei; Chiu, Wei-Jane; Wei, Tsao-Yen; Roy, Prathik; Huang, Chih-Ching

2012-04-21

We have developed a simple, low-cost, paper-based probe for the selective colorimetric detection of copper ions (Cu(2+)) in aqueous solutions. The bovine serum albumin (BSA)-modified 13.3-nm Au nanoparticle (BSA-Au NP) probe was designed to detect Cu(2+) ions using lead ions (Pb(2+)) and 2-mercaptoethanol (2-ME) as leaching agents in a glycine-NaOH (pH 12.0) solution. In addition, a nitrocellulose membrane (NCM) was used to trap the BSA-Au NPs, leading to the preparation of a nanocomposite film consisting of a BSA-Au NP-decorated membrane (BSA-Au NPs/NCM). The BSA-Au NPs probe operates on the principle that Cu deposition on the surface of the BSA-Au NPs inhibits their leaching ability, which is accelerated by Pb(2+) ions in the presence of 2-ME. Under optimal solution conditions (5 mM glycine-NaOH (pH 12.0), Pb(2+) (50 μM), and 2-ME (1.0 M)), the Pb(2+)/2-ME-BSA-Au NPs/NCM enabled the detection of Cu(2+) at nanomolar concentrations in aqueous solutions by the naked eye with high selectivity (at least 100-fold over other metal ions). In addition, this cost-effective probe allowed for the rapid and simple determination of Cu(2+) ions in not only natural water samples but also in a complex biological sample (in this case, blood sample).

Interaction studies of resistomycin from Streptomyces aurantiacus AAA5 with calf thymus DNA and bovine serum albumin

Science.gov (United States)

Vijayabharathi, R.; Sathyadevi, P.; Krishnamoorthy, P.; Senthilraja, D.; Brunthadevi, P.; Sathyabama, S.; Priyadarisini, V. Brindha

2012-04-01

Resistomycin, a secondary metabolite produced by Streptomyces aurantiacus AAA5. The binding interaction of resistomycin with calf thymus DNA (CT DNA) and bovine serum albumin (BSA) was investigated by spectrophotometry, spectrofluorimetry, circular dichroism (CD) and synchronous fluorescence techniques under physiological conditions in vitro. Absorption spectral studies along with the fluorescence competition with ethidium bromide measurements and circular dichroism clearly suggest that the resistomycin bind with CT DNA relatively strong via groove binding. BSA interaction results revealed that the drug was found to quench the fluorescence intensity of the protein through a static quenching mechanism. The number of binding sites 'n' and apparent binding constant 'K' calculated according to the Scatchard equation exhibit a good binding property to bovine serum albumin protein. In addition, the results observed from synchronous fluorescence measurements clearly demonstrate the occurrence of conformational changes of BSA upon addition of the test compound.

Spectroscopic Studies on the Interaction of Acid Yellow With Bovine Serum Albumin

International Nuclear Information System (INIS)

Pan Xingren; Liu Rutao; Qin Pengfei; Wang Li; Zhao Xingchen

2010-01-01

Azo dyes, which are common in the environment, can be toxic to various organisms. In order to determine the molecular mechanism of acid yellow 11(AY) toxicity, we studied the effect of AY exposure to the common protein bovine serum albumin (BSA) by several spectroscopic techniques including fluorescence spectroscopy, ultraviolet spectrophotometry (UV) and circular dichroism (CD). It could be concluded from the fluorescence spectra that the quenching effect of BSA by AY was mainly due to complex formation which was unrelated to the absorption of AY. The enthalpy change (ΔH) and entropy change (ΔS) were found to be -21.94 kJ/mol and 30.04 Jmol -1 K -1 , respectively. The results confirm that electrostatic attraction was the predominant intermolecular force between BSA and AY. Furthermore, the binding distance (r) between AY and the inner tryptophan residue of BSA was determined to be 3.541 nm on the basis of Forster theory of non-radiative energy transfer. In addition, the conformational changes of BSA in the presence of AY were also analyzed by UV and CD. These results indicated that AY could interact with BSA by complex formation, which also affected the structure of BSA.

Formation and Properties of Multilayer Films Based on Polyethyleneimine and Bovine Serum Albumin

Science.gov (United States)

Kulikouskaya, V. I.; Lazouskaya, M. E.; Kraskouski, A. N.; Agabekov, V. E.

2018-01-01

(Polyethyleneimine/bovine serum albumin) n ((PEI/BSA) n) multilayer films ( n = 1-10) are produced via the layer-by-later deposition of polyelectrolytes. It is shown that thickness and morphology of the formed coatings can be controlled by varying the solution's ionic strength during alternating adsorption of the components. (PEI/BSA)10 multilayer systems that contain up to 0.6 mg of antiseptic miramistin per 1 cm2 of film were created. It is established that the kinetics of miramistin release from (PEI/BSA)10 films in phosphate buffers and physiological solutions obey the Korsmeyer-Peppas equation with a high degree of accuracy ( R 2 > 0.95).

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...

Albumin's Influence on Carprofen Enantiomers-Hymecromone Interaction.

Science.gov (United States)

Tang, Mingjie; Guo, Yanjie; Gao, Youshui; Tang, Chao; Dang, Xiaoqian; Zhou, Zubin; Sun, Yuqiang; Wang, Kunzheng

2016-03-01

Hymecromone is an important coumarin drug, and carprofen is one of the most important nonsteroidal antiinflammatory drugs (NSAIDs). The present study aims to determine the influence of bovine serum albumin (BSA) on the carprofen-hymecromone interaction. The inhibition of carprofen enantiomers on the UDP-glucuronosyltransferase (UGT) 2B7-catalyzed glucuronidation of hymecromone was investigated in the UGTs incubation system with and without BSA. The inhibition capability of increased by 20% (P carprofen after the addition of 0.5% BSA in the incubation mixture. In contrast, no significant difference was observed for the inhibition of (S)-carprofen on UGT2B7 activity in the absence or presence of 0.5% BSA in the incubation system. The Lineweaver-Burk plot showed that the intersection point was located in the vertical axis, indicating the competitive inhibition of (R)-carprofen on UGT2B7 in the incubation system with BSA, which is consistent with the inhibition kinetic type of (R)-carprofen on UGT2B7 in the incubation system without BSA. Furthermore, the second plot using the slopes from the Lineweaver-Burk versus the concentrations of (R)-carprofen showed that the fitting equation was y=39.997x+50. Using this equation, the inhibition kinetic parameter was calculated to be 1.3 μM. For (S)-carprofen, the intersection point was located in the horizontal axis in the Lineweaver-Burk plot for the incubation system with BSA, indicating the noncompetitive inhibition of (S)-carprofen on the activity of UGT2B7. The fitting plot of the second plot was y=24.6x+180, and the inhibition kinetic parameter was 7.3 μM. In conclusion, the present study gives a short summary of BSA's influence on the carprofen enantiomers-hymecromone interaction, which will guide the clinical application of carprofen and hymecromone. © 2015 Wiley Periodicals, Inc.

Antioxidant flavone analog functionalized fluorescent silica nanoparticles: Synthesis and exploration of their possible use as biomolecule sensor.

Science.gov (United States)

Das, Sreeparna; Batuta, Shaikh; Alam, Md Niharul; Fouzder, Chandrani; Kundu, Rakesh; Mandal, Debabrata; Begum, Naznin Ara

2017-09-01

For the first time, a synthetic fluorescent antioxidant flavone analog was successfully anchored onto the surface of the APTES-modified mesoporous silica nanoparticles (NPs) through sulfonamide linkage. The surface chemistry and morphology of the flavone modified fluorescent silica (FMFS) NPs were studied in detail. The flavone moiety when attached onto the FMFS NP surface, imparted its characteristic fluorescence and antioxidant activities to these NPs. Moreover, the NPs are highly biocompatible as evidenced from their cytotoxicity assay on normal lung cell (L132). The fluorescence activity of these biocompatible NPs was further utilized to study their interaction with a biomolecule, BSA (Bovine Serum Albumin). It was interesting to note that the fluorescence behavior of FMFS NPs completely changed on their binding with BSA. On the other hand, the intrinsic fluorescence activity of BSA was also significantly modified due to its interaction with FMFS NPs. Thus, the sensing and detection of biomolecules like BSA in presence of FMFS NPs can be accomplished by monitoring changes in the fluorescence behavior of either FMFS NPs or BSA. Furthermore, these FMFS NPs retained their intrinsic fluorescence behavior in the cellular medium which opens up their possible use as biocompatible cell imaging agents in future. Copyright © 2017 Elsevier B.V. All rights reserved.

Analysis of the hydration water around bovine serum albumin using terahertz coherent synchrotron radiation.

Science.gov (United States)

Bye, Jordan W; Meliga, Stefano; Ferachou, Denis; Cinque, Gianfelice; Zeitler, J Axel; Falconer, Robert J

2014-01-09

Terahertz spectroscopy was used to study the absorption of bovine serum albumin (BSA) in water. The Diamond Light Source operating in a low alpha mode generated coherent synchrotron radiation that covered a useable spectral bandwidth of 0.3-3.3 THz (10-110 cm(-1)). As the BSA concentration was raised, there was a nonlinear change in absorption inconsistent with Beer's law. At low BSA concentrations (0-1 mM), the absorption remained constant or rose slightly. Above a concentration of 1 mM BSA, a steady decrease in absorption was observed, which was followed by a plateau that started at 2.5 mM. Using a overlapping hydration layer model, the hydration layer was estimated to extend 15 Å from the protein. Calculation of the corrected absorption coefficient (αcorr) for the water around BSA by subtracting the excluded volume of the protein provides an alternative approach to studying the hydration layer that provides evidence for complexity in the population of water around BSA.

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.

Pulse radiolytic and spectrophotometric investigation of the binding of bilirubin to bovine serum albumin

International Nuclear Information System (INIS)

Adhikari, S.; Guha, S.N.; Gopinathan, C.

1994-01-01

Bilirubin (BR) exhibits marked change in its absorption properties in the presence of bovine serum albumin (BSA). The λ max of BR observed at 440 nm is red shifted by about 20 nm with 8% increase in band intensity when BSA is present in the matrix. Medium polarity and salt effects were also studied in this system and it was inferred that BR is bound to BSA to form a complex, which becomes unstable at high salt concentration or in a medium of low dielectric constant such as water-alcohol mixture. Pulse radiolysis study of this system employing CO 2 .- radical revealed that BR blocks the sites of CO 2 .- attack in the BSA molecule. (author). 3 refs., 2 figs

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.

Characterize the interaction between naringenin and bovine serum albumin using spectroscopic approach

International Nuclear Information System (INIS)

Hu Yanjun; Wang Yang; Ouyang Yu; Zhou Juan; Liu Yi

2010-01-01

Naringenin, a flavanone compound highly enriched in grapefruits, has been identified as a possible inhibitor of cell proliferation; and thus has the potential to act as an antitumorigenic agent. In this study, the binding of naringenin to bovine serum albumin (BSA) was studied at the physiological conditions (pH=7.40) by fluorescence and UV-vis spectroscopy. Naringenin strongly quenches the intrinsic fluorescence of BSA, and a decrease in the fluorescence quenching constant was observed together with an increase in temperature, which indicates that the fluorescence quenching of BSA by naringenin is a result of the formation of naringenin-BSA complex. Binding parameters calculating from Stern-Volmer method and Scatchard method showed that naringenin bind to BSA with the binding affinities of the order 10 4 L mol -1 . Thermodynamic parameters such as ΔG, ΔH and ΔS, were calculated at different temperatures, showing that electrostatic interactions were mostly responsible for the binding of naringenin to BSA. Site marker competitive displacement experiments demonstrating that naringenin bind with high affinity to site I (subdomain IIA) of BSA. Furthermore, the effect of metal ions to naringenin-BSA system was studied, and the specific binding distance r (3.30 nm) between donor (Trp-212) and acceptor (naringenin) was obtained according to fluorescence resonance energy transfer (FRET).

Biophysical influence of coumarin 35 on bovine serum albumin: Spectroscopic study

Science.gov (United States)

Bayraktutan, Tuğba; Onganer, Yavuz

2017-01-01

The binding mechanism and protein-fluorescence probe interactions between bovine serum albumin (BSA) and coumarin 35 (C35) was investigated by using UV-Vis absorption and fluorescence spectroscopies since they remain major research topics in biophysics. The spectroscopic data indicated that a fluorescence quenching process for BSA-C35 system was occurred. The fluorescence quenching processes were analyzed using Stern-Volmer method. In this regard, Stern-Volmer quenching constants (KSV) and binding constants were calculated at different temperatures. The distance r between BSA (donor) and C35 (acceptor) was determined by exploiting fluorescence resonance energy transfer (FRET) method. Synchronous fluorescence spectra were also studied to observe information about conformational changes. Moreover, thermodynamics parameters were calculated for better understanding of interactions and conformational changes of the system.

Spectroscopic studies on the binding of barbital to bovine serum albumin

Energy Technology Data Exchange (ETDEWEB)

Ding Fei, E-mail: caudf@163.co [Department of Chemistry, China Agricultural University, Beijing 100193 (China); Pan Hong; Li Zhiyuan; Liu Feng [Department of Chemistry, China Agricultural University, Beijing 100193 (China); Sun Ying, E-mail: sunying@cau.edu.c [Department of Chemistry, China Agricultural University, Beijing 100193 (China)

2009-06-15

In this paper, the interaction between barbital and bovine serum albumin (BSA) was investigated by the method of fluorescence spectroscopy under simulative physiological conditions. Fluorescence data revealed that the fluorescence quenching of BSA by barbital was the result of the formation of BSA-barbital complex, and the effective quenching constants (K{sub a}) were 1.468x10{sup 4}, 1.445x10{sup 4} and 1.403x10{sup 4} M{sup -1} at 297, 303 and 310 K, respectively. The thermodynamic parameters enthalpy change (DELTAH) and entropy change (DELTAS) for the reaction were calculated to be -2.679 kJ mol{sup -1} and 70.76 J mol{sup -1} K{sup -1}, respectively, according to the van't Hoff equation. The results indicated that hydrophobic and electrostatic interactions were the dominant intermolecular force in stabilizing the complex. The results of synchronous fluorescence spectra showed that binding of barbital with BSA can induce conformational changes in BSA. In addition, the effects of Cu{sup 2+} and Zn{sup 2+} on the constants of BSA-barbital complex were also discussed.

Improved delivery of the anticancer agent citral using BSA nanoparticles and polymeric wafers

Directory of Open Access Journals (Sweden)

White B

2017-12-01

Full Text Available Benjamin White,1 Anna Evison,1 Eszter Dombi,1 Helen E Townley1,2 1Nuffield Department of Obstetrics and Gynaecology, Women’s Centre, John Radcliffe Hospital, 2Department of Engineering Science, Oxford University, Oxford, UK Abstract: Rhabdomyosarcoma (RMS is the most common soft tissue sarcoma in children, with a 5-year survival rate of between 30 and 65%. Standard treatment involves surgery, radiation treatment, and chemotherapy. However, there is a high recurrence rate, particularly from locoregional spread. We investigated the use of the natural compound citral (3,7-dimethyl-2,6-octadienal, which can be found in a number of plants, but is particularly abundant in lemon grass (Cymbopogon citratus oil, for activity against immortalized RMS cells. Significant cancer cell death was seen at concentrations above 150 μM citral, and mitochondrial morphological changes were seen after incubation with 10 μM citral. However, since citral is a highly volatile molecule, we prepared albumin particles by a desolvation method to encapsulate citral, as a means of stabilization. We then further incorporated the loaded nanoparticles into a biodegradable polyanhydride wafer to generate a slow release system. The wafers were shown to degrade by 50% over the course of 25 days and to release the active compound. We therefore propose the use of the citral-nanoparticle-polymer wafers for implantation into the tumor bed after surgical removal of a sarcoma as a means to control locoregional spread due to any remaining cancerous cells. Keywords: citral, nanoparticle, wafer, biodegradable, mitochondria, toroidal, cancer, rhabdomyosarcoma, Cymbopogon citratus

Investigations into the oxygen effect during the radiolysis of serum albumin with the help of SDS-polyacrylamide gel electrophoresis

International Nuclear Information System (INIS)

Schilling, K.B.G.

1984-01-01

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) [de

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

International Nuclear Information System (INIS)

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

2013-01-01

TiO 2 nanoparticles (NPs) are contained in different kinds of industrial products including paints, self-cleaning glasses, sunscreens. TiO 2 is also employed in photocatalysis and it has been proposed for waste water treatment. Micrometric TiO 2 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 TiO 2 nanoparticles of different crystal phases (rutile and anatase) using an integrated set of techniques. The amount of adsorbed fibrinogen and albumin for each TiO 2 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

Investigation on the pH-dependent binding of Eosin Y and bovine serum albumin by spectral methods

International Nuclear Information System (INIS)

Gao Dejiang; Tian Yuan; Liang Fanghui; Jin Danhong; Chen Yanhua; Zhang Hanqi; Yu Aimin

2007-01-01

In this paper, the pH-dependent binding of Eosin Y and bovine serum albumin (BSA) was investigated by spectral methods, including resonance light scattering (RLS), absorption and fluorescence spectrometry. Due to the pH-dependent structure of Eosin Y and BSA, the interaction of BSA and Eosin Y depended on the solution pH value. Especially at pH 2.6 and 9.2, the RLS intensity of BSA was obviously enhanced in the presence of Eosin Y. However, the fluorescence intensity of BSA was quenched in the presence of Eosin Y. To fully understand the pH-dependent binding of BSA and Eosin Y, fluorescence quenching technique was introduced. Based on the fluorescence data obtained, the style of binding, the binding constant, the binding site number and the thermodynamic parameters for the interaction of BSA and Eosin Y were studied. Based on Foerster non-radiation energy transfer theory, the distance between donor BSA and acceptor Eosin Y was obtained

Investigation on the pH-dependent binding of Eosin Y and bovine serum albumin by spectral methods

Energy Technology Data Exchange (ETDEWEB)

Gao Dejiang; Tian Yuan [College of Chemistry, Jilin University, Changchun 130012 (China); Liang Fanghui; Jin Danhong [Changchun Medical College, Changchun 130031 (China); Chen Yanhua; Zhang Hanqi [College of Chemistry, Jilin University, Changchun 130012 (China); Yu Aimin [College of Chemistry, Jilin University, Changchun 130012 (China)], E-mail: analchem@mail.jlu.edu.cn

2007-12-15

In this paper, the pH-dependent binding of Eosin Y and bovine serum albumin (BSA) was investigated by spectral methods, including resonance light scattering (RLS), absorption and fluorescence spectrometry. Due to the pH-dependent structure of Eosin Y and BSA, the interaction of BSA and Eosin Y depended on the solution pH value. Especially at pH 2.6 and 9.2, the RLS intensity of BSA was obviously enhanced in the presence of Eosin Y. However, the fluorescence intensity of BSA was quenched in the presence of Eosin Y. To fully understand the pH-dependent binding of BSA and Eosin Y, fluorescence quenching technique was introduced. Based on the fluorescence data obtained, the style of binding, the binding constant, the binding site number and the thermodynamic parameters for the interaction of BSA and Eosin Y were studied. Based on Foerster non-radiation energy transfer theory, the distance between donor BSA and acceptor Eosin Y was obtained.

Biomimetic coprecipitation of calcium phosphate and bovine serum albumin on titanium alloy

NARCIS (Netherlands)

Liu, Yuelian; Layrolle, Pierre; de Bruijn, Joost Dick; van Blitterswijk, Clemens; de Groot, K.

2001-01-01

Titanium alloy implants were precoated biomimetically with a thin and dense layer of calcium phosphate and then incubated either in a supersaturated solution of calcium phosphate or in phosphate-buffered saline, each containing bovine serum albumin (BSA) at various concentrations, under

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. Copyright © 2013 Elsevier Ltd. All rights reserved.

Biocompatible capped iron oxide nanoparticles for Vibrio cholerae detection

International Nuclear Information System (INIS)

Sharma, Anshu; Rawat, Kamla; Solanki, Pratima R; Bohidar, H B; Baral, Dinesh

2015-01-01

We report the studies relating to fabrication of an efficient immunosensor for Vibrio cholerae detection. Magnetite (iron oxide (Fe 3 O 4 )) 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 Fe 3 O 4 and CA-Fe 3 O 4 /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 Fe 3 O 4 , CA-Fe 3 O 4 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 (Fe 3 O 4 ) and 189.51 nm (CA-Fe 3 O 4 ) by DLS measurement. The results of electrochemical response studies of the fabricated BSA/Ab/CA-Fe 2 O 3 /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. (paper)

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.

Quantitative aspects of recognition of the antibiotic drug oxytetracycline by bovine serum albumin: Calorimetric and spectroscopic studies

Energy Technology Data Exchange (ETDEWEB)

Keswani, Neelam; Choudhary, Sinjan [Department of Chemistry, Indian Institute of Technology Bombay, Powai, Mumbai 400 076 (India); Kishore, Nand [Department of Chemistry, Indian Institute of Technology Bombay, Powai, Mumbai 400 076 (India)

2013-03-15

Highlights: ► Thermodynamics of oxytetracycline (OTC)-bovine serum albumin (BSA) binding addressed. ► ITC and fluorescence spectroscopic analysis provide values of binding constant. ► Binding is mainly ionic, hydrophobic with minor hydrogen bonding contribution. ► Quantitative effects of OTC on BSA stability provided by DSC. ► Preferential complexation of one domain of BSA by OTC at site II is suggested. -- Abstract: A quantitative understanding of the mode of interaction of drugs with target proteins provides a guide for the synthesis of new drug molecules. The binding of the antibiotic drug oxytetracycline with serum albumin has been studied by a combination of isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC), steady-state and time-resolved fluorescence spectroscopy, and circular dichroism spectroscopy. The values of the binding constant (K), enthalpy change (ΔH), entropy (ΔS), and stoichiometry of binding have been determined along with the associated conformational changes in the protein. Oxytetracycline binds to bovine serum albumin with a 1:1 stoichiometry and with a weakly temperature dependent association constant of 1.8 · 10{sup 4} at T = 298.15 K. The effect of ionic strength, tetrabutylammonium bromide, and sucrose on the thermodynamic parameters obtained from ITC and DSC measurements indicate involvement of predominantly ionic and hydrophobic interactions with a minor hydrogen bonding contribution in the drug-protein complexation. The DSC results on the binding of oxytetracycline with bovine serum albumin in the absence and presence of these additives provide quantitative information on the effect of drugs on the stability of bovine serum albumin, and suggest preferential complexation of one of the domains of the protein. The results further indicate that the drug occupies binding site II on bovine serum albumin.

Quantitative aspects of recognition of the antibiotic drug oxytetracycline by bovine serum albumin: Calorimetric and spectroscopic studies

International Nuclear Information System (INIS)

Keswani, Neelam; Choudhary, Sinjan; Kishore, Nand

2013-01-01

Highlights: ► Thermodynamics of oxytetracycline (OTC)-bovine serum albumin (BSA) binding addressed. ► ITC and fluorescence spectroscopic analysis provide values of binding constant. ► Binding is mainly ionic, hydrophobic with minor hydrogen bonding contribution. ► Quantitative effects of OTC on BSA stability provided by DSC. ► Preferential complexation of one domain of BSA by OTC at site II is suggested. -- Abstract: A quantitative understanding of the mode of interaction of drugs with target proteins provides a guide for the synthesis of new drug molecules. The binding of the antibiotic drug oxytetracycline with serum albumin has been studied by a combination of isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC), steady-state and time-resolved fluorescence spectroscopy, and circular dichroism spectroscopy. The values of the binding constant (K), enthalpy change (ΔH), entropy (ΔS), and stoichiometry of binding have been determined along with the associated conformational changes in the protein. Oxytetracycline binds to bovine serum albumin with a 1:1 stoichiometry and with a weakly temperature dependent association constant of 1.8 · 10 4 at T = 298.15 K. The effect of ionic strength, tetrabutylammonium bromide, and sucrose on the thermodynamic parameters obtained from ITC and DSC measurements indicate involvement of predominantly ionic and hydrophobic interactions with a minor hydrogen bonding contribution in the drug-protein complexation. The DSC results on the binding of oxytetracycline with bovine serum albumin in the absence and presence of these additives provide quantitative information on the effect of drugs on the stability of bovine serum albumin, and suggest preferential complexation of one of the domains of the protein. The results further indicate that the drug occupies binding site II on bovine serum albumin

Study of the interaction of kaempferol with bovine serum albumin

Science.gov (United States)

Tian, Jianniao; Liu, Jiaqin; Tian, Xuan; Hu, Zhide; Chen, Xingguo

2004-03-01

The binding of kaempferol with bovine serum albumin (BSA) was investigated at three temperatures, 296, 310 and 318 K, by the fluorescence, circular dichroism (CD) and Fourier transform infrared spectroscopy (FT-IR) at pH 7.40. The CD and FT-IR studies indicate that kaempferol binds strongly to BSA. The association constant K was determined by Stern-Volmer equation based on the quenching of the fluorescence BSA in the presence of kaempferol. The thermodynamic parameters were calculated according to the dependence of enthalpy change on the temperature as follows: Δ H0 and Δ S0 possess small negative (-1.694 kJ/mol) and positive values (88.814 J/mol K), respectively. According to the displacement experimental and the thermodynamic results, it is considered that kaempferol binding site II (subdomain III) mainly by hydrophobic interaction. The results studied by FT-IR and CD experiments indicate that the secondary structures of the protein have been changed by the interaction of kaempferol with BSA. The distance between the tryptophan residues in BSA and kaempferol bound to site II was estimated to be 2.78 nm using Foster's equation on the basis of fluorescence energy transfer.

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

International Nuclear Information System (INIS)

Teng Yue; Liu Rutao; Li Chao; Xia Qing; Zhang Pengjun

2011-01-01

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.

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.

Multi-spectroscopic characterization of bovine serum albumin upon interaction with atomoxetine

Directory of Open Access Journals (Sweden)

Arunkumar T. Buddanavar

2017-06-01

Full Text Available The quenching interaction of atomoxetine (ATX with bovine serum albumin (BSA was studied in vitro under optimal physiological condition (pH=7.4 by multi-spectroscopic techniques. The mechanism of ATX-BSA system was a dynamic quenching process and was confirmed by the fluorescence spectra and lifetime measurements. The number of binding sites, binding constants and other binding characteristics were computed. Thermodynamic parameters ∆H° and ∆S° indicated that intermolecular hydrophobic forces predominantly stabilized the drug-protein system. The average binding distance between BSA and ATX was studied by Försters theory. UV-absorption, Fourier transform infrared spectroscopy (FT-IR, circular dichroism (CD, synchronous spectra and three-dimensional (3D fluorescence spectral results revealed the changes in micro-environment of secondary structure of protein upon the interaction with ATX. Displacement of site probes and the effects of some common metal ions on the binding of ATX with BSA interaction were also studied.

Coupling of albumin flux to volume flow in skin and muscles of anesthetized rats

International Nuclear Information System (INIS)

Renkin, E.M.; Gustafson-Sgro, M.; Sibley, L.

1988-01-01

Bovine serum albumin (BSA) labeled with 131 I or 125 I 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

Uptake and cytotoxicity of poly(D,L-lactide-co-glycolide) nanoparticles in human colon adenocarcinoma cells

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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.

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

International Nuclear Information System (INIS)

Li, Xu; Jiang, Jian-Hong; Xiao, Sheng-Xiong; Gu, Hui-Wen; Li, Chuan-Hua; Ye, Li-Juan; Li, Xia; He, Du-Gui; Yao, Fei-Hong; Li, Qiang-Guo

2014-01-01

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 22 H 24 N 4 O 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 f H m Θ [C 22 H 24 N 4 O 5 (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

Spectroscopic investigation on the interaction of titanate nanotubes with bovine serum albumin

International Nuclear Information System (INIS)

Zhao, L.Z.; Zhao, Y.S.; Teng, H.H.; Shi, S.Y.; Ren, B.X.

2014-01-01

In order to understand the transport mechanism and evaluate the biological safety of titanate nanotubes, the interactions of titanate nanotubes (TNTs) with bovine serum albumin (BSA) were investigated by applying spectroscopic methods under simulated physiological conditions. After taking into account the inner filter effect, the fluorescence intensity of BSA was found to be significantly enhanced by the presence of TNTs, indicating that the microenvironment of tryptophan and tyrosine residues in BSA became more hydrophobic. In addition, the absorption spectra of BSA showed a hyperchromic effect around 280 nm as the concentration of TNTs increased, suggesting that TNTs changed the microenvironment of the tryptophan and tyrosine residues. This is consistent with the results from fluorescence spectroscopy studies. However, circular dichroism spectroscopy revealed that no significant conformational change in BSA occurred during the interaction. We believe that Trp-213 was buried more compactly in the internal hydrophobic region, and hydrophobicity increased around Trp-134 with increasing TNTs concentration. From a spectroscopic point of view, this work elucidates the interaction mechanism of titanate nanotubes with BSA, and the methods used in this paper can also be applied to explore the molecular mechanism underlying toxicity of other nanomaterials. (authors)

Role of pH-induced structural change in protein aggregation in foam fractionation of bovine serum albumin

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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.

Phenytoin-Bovine Serum Albumin interactions - modeling plasma protein - drug binding: A multi-spectroscopy and in silico-based correlation

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Suresh, P. K.; Divya, Naik; Nidhi, Shah; Rajasekaran, R.

2018-03-01

The study focused on the analysis of the nature and site of binding of Phenytoin (PHT) -(a model hydrophobic drug) with Bovine Serum Albumin (BSA) (a model protein used as a surrogate for HSA). Interactions with defined amounts of Phenytoin and BSA demonstrated a blue shift (hypsochromic -change in the microenvironment of the tryptophan residue with decrease in the polar environment and more of hydrophobicity) with respect to the albumin protein and a red shift (bathochromic -hydrophobicity and polarity related changes) in the case of the model hydrophobic drug. This shift, albeit lower in magnitude, has been substantiated by a fairly convincing, Phenytoin-mediated quenching of the endogenous fluorophore in BSA. Spectral shifts studied at varying pH, temperatures and incubation periods (at varying concentrations of PHT with a defined/constant BSA concentration) showed no significant differences (data not shown). FTIR analysis provided evidence of the interaction of PHT with BSA with a stretching vibration of 1737.86 cm- 1, apart from the vibrations characteristically associated with the amine and carboxyl groups respectively. Our in vitro findings were extended to molecular docking of BSA with PHT (with the different ionized forms of the drug) and the subsequent LIGPLOT-based analysis. In general, a preponderance of hydrophobic interactions was observed. These hydrophobic interactions corroborate the tryptophan-based spectral shifts and the fluorescence quenching data. These results substantiates our hitherto unreported in vitro/in silico experimental flow and provides a basis for screening other hydrophobic drugs in its class.

Increasing the X-ray Diffraction Power of Protein Crystals by Dehydration: The Case of Bovine Serum Albumin and a Survey of Literature Data

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Irene Russo Krauss

2012-03-01

Full Text Available Serum albumin is one of the most widely studied proteins. It is the most abundant protein in plasma with a typical concentration of 5 g/100 mL and the principal transporter of fatty acids in plasma. While the crystal structures of human serum albumin (HSA free and in complex with fatty acids, hemin, and local anesthetics have been characterized, no crystallographic models are available on bovine serum albumin (BSA, presumably because of the poor diffraction power of existing hexagonal BSA crystals. Here, the crystallization and diffraction data of a new BSA crystal form, obtained by the hanging drop method using MPEG 5K as precipitating agent, are presented. The crystals belong to space group C2, with unit-cell parameters a = 216.45 Å, b = 44.72 Å, c = 140.18 Å, β = 114.5°. Dehydration was found to increase the diffraction limit of BSA crystals from ~8 Å to 3.2 Å, probably by improving the packing of protein molecules in the crystal lattice. These results, together with a survey of more than 60 successful cases of protein crystal dehydration, confirm that it can be a useful procedure to be used in initial screening as a method of improving the diffraction limits of existing crystals.

Development of Cy5.5-Labeled Hydrophobically Modified Glycol Chitosan Nanoparticles for Protein Delivery

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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.

Fluorescence lifetime measurements of native and glycated human serum albumin and bovine serum albumin

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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.

Measurement of the average mass of proteins adsorbed to a nanoparticle by using a suspended microchannel resonator.

Science.gov (United States)

Nejadnik, M Reza; Jiskoot, Wim

2015-02-01

We assessed the potential of a suspended microchannel resonator (SMR) to measure the adsorption of proteins to nanoparticles. Standard polystyrene beads suspended in buffer were weighed by a SMR system. Particle suspensions were mixed with solutions of bovine serum albumin (BSA) or monoclonal human antibody (IgG), incubated at room temperature for 3 h and weighed again with SMR. The difference in buoyant mass of the bare and protein-coated polystyrene beads was calculated into real mass of adsorbed proteins. The average surface area occupied per protein molecule was calculated, assuming a monolayer of adsorbed protein. In parallel, dynamic light scattering (DLS), nanoparticle tracking analysis (NTA), and zeta potential measurements were performed. SMR revealed a statistically significant increase in the mass of beads because of adsorption of proteins (for BSA and IgG), whereas DLS and NTA did not show a difference between the size of bare and protein-coated beads. The change in the zeta potential of the beads was also measurable. The surface area occupied per protein molecule was in line with their known size. Presented results show that SMR can be used to measure the mass of adsorbed protein to nanoparticles with a high precision in the presence of free protein. © 2014 Wiley Periodicals, Inc. and the American Pharmacists Association.

Sample preconcentration utilizing nanofractures generated by junction gap breakdown assisted by self-assembled monolayer of gold nanoparticles.

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Chun-Ping Jen

Full Text Available The preconcentration of proteins with low concentrations can be used to increase the sensitivity and accuracy of detection. A nonlinear electrokinetic flow is induced in a nanofluidic channel due to the overlap of electrical double layers, resulting in the fast accumulation of proteins, referred to as the exclusion-enrichment effect. The proposed chip for protein preconcentration was fabricated using simple standard soft lithography with a polydimethylsiloxane replica. This study extends our previous paper, in which gold nanoparticles were manually deposited onto the surface of a protein preconcentrator. In the present work, nanofractures were formed by utilizing the self-assembly of gold-nanoparticle-assisted electric breakdown. This reliable method for nanofracture formation, involving self-assembled monolayers of nanoparticles at the junction gap between microchannels, also decreases the required electric breakdown voltage. The experimental results reveal that a high concentration factor of 1.5×10(4 for a protein sample with an extremely low concentration of 1 nM was achieved in 30 min by using the proposed chip, which is faster than our previously proposed chip at the same conditions. Moreover, an immunoassay of bovine serum albumin (BSA and anti-BSA was carried out to demonstrate the applicability of the proposed chip.

[Preparation and performance characterization of gold nanoparticles modified chiral capillary electrochromatography stationary phase].

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Xiong, Lele; Li, Ruijun; Ji, Yibing

2017-07-08

Gold nanoparticles (GNPs, 15 nm) were prepared and introduced to amino groups derived silica monolithic column. Bovine serum albumin (BSA) was immobilized via covalent modification method onto the carboxylic functionalized GNPs to afford chiral stationary phase (CSP) for enantioseparation. GNPs were well dispersed and successfully incorporated onto the columns with the contents as high as 17.18% by characterization method such as transmission electron microscopy (TEM), ultraviolet (UV)-visible absorption spectra and scanning electron microscopy (SEM). The preparation conditions of the BSA modified CSP were optimized and 10% (v/v) 3-aminopropyltriethoxysilane (APTES) and 15 g/L BSA were selected as appropriate reaction conditions. The enantioseparation performance of the BSA modified CSP has been investigated by capillary electrochromatography (CEC). Enantiomers of tryptophan, ephedrine and atenolol were resolved, and the baseline separation of tryptophan was achieved. Meanwhile, the influences of pH value, buffer concentrations and applied voltages used on the chiral separation were studied, and the optimal separation conditions were 10 mmol/L phosphate buffer at pH 7.4 and 15 kV applied voltages. In comparison with the BSA modified CSP prepared by physical adsorption, the CSP prepared by covalent modification method had better separation results, and the analytes could be separated directly without pre-column derivatization. In addition, the prepared BSA modified CSP exhibited good run to run repeatability with relative standard deviations (RSDs) of the migration times and selectivity factors not more than 2.3% and 0.96%, respectively. This work offers a good thinking for modification with other proteins or other types of chiral selectors.

Increased osteoblast density in the presence of novel calcium phosphate coated magnetic nanoparticles

International Nuclear Information System (INIS)

Pareta, Rajesh A; Webster, Thomas J; Taylor, Erik

2008-01-01

Bone diseases (including osteoporosis, osteoarthritis and bone cancer) are of great concern to the medical world. Drugs are available to treat such diseases, but often these drugs are not specifically targeted to the site of the disease and, thus, lack an immediate directed therapeutic effect. The optimal drug delivery system should enhance healthy bone growth with high specificity to the site of bone disease. It has been previously shown that magnetic nanoparticles can be directed in the presence of a magnetic field to any part of the body, allowing for site-specific drug delivery and possibly an immediate increase in bone density. The objective of the present study was to build off of this evidence and determine the density of osteoblasts (bone forming cells) in the presence of various uncoated and coated magnetic nanoparticles that could eventually be used in drug delivery applications. Results showed that some magnetic nanoparticles (specifically, γ-Fe 2 O 3 ) significantly promoted osteoblast density (that is, cells per well) after 5 and 8 days of culture compared to controls (no particles). These magnetic nanoparticles were further coated with calcium phosphate (CaP; the main inorganic component of bone) to tailor them for treating various bone diseases. The coatings were conducted in the presence of either bovine serum albumin (BSA) or citric acid (CA) to reduce magnetic nanoparticle agglomeration, a common problem resulting from the use of nanoparticles which decreases their effectiveness. Results with these coatings showed that magnetic nanoparticles, specifically (γ-Fe 2 O 3 ), coated in the presence of BSA significantly increased osteoblast density compared to controls after 1 day. In this manner, this study provided unexpected evidence that CaP-coated γ-Fe 2 O 3 magnetic nanoparticles increased osteoblast density (compared to no particles) and, thus, should be further studied to treat numerous bone diseases

Constrained Photophysics of 5,7-dimethoxy-2,3,4,9-tetrahydro-1H-carbazol-1-one in the Bioenvironment of Serum Albumins: A Spectroscopic Endeavour Supported by Molecular Docking Analysis.

Science.gov (United States)

Mitra, Amrit Krishna; Sau, Abhishek; Pal, Uttam; Saha, Chandan; Basu, Samita

2017-07-01

This paper vividly indicates that steady state as well as time-resolved fluorescence techniques can serve as highly sensitive monitors to explore the interactions of 5,7-dimethoxy-2,3,4,9-tetrahydro-1H-carbazol-1-one with model transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA). Besides these, we have used fluorescence anisotropy study to assess the degree of restrictions imparted by the micro-environments of serum albumins. Again, to speculate the triplet excited state interaction between such fluorophore and albumin proteins (BSA& HSA), laser flash-photolysis experiments have been carried out. Molecular docking experiments have also been performed to support the conclusions obtained from steady state experiments.

Binding of ethyl pyruvate to bovine serum albumin: Calorimetric, spectroscopic and molecular docking studies

Energy Technology Data Exchange (ETDEWEB)

Pathak, Mallika [Department of Chemistry, Miranda House, University of Delhi, Delhi 11007 (India); Mishra, Rashmi; Agarwala, Paban K. [Department of Radiation Genetics and Epigenetics, Division of Radioprotective Drug Development Research, Institute of Nuclear Medicine and Allied Sciences, Delhi 110054 (India); Ojha, Himanshu, E-mail: himanshu.drdo@gmail.com [Department of Radiation Genetics and Epigenetics, Division of Radioprotective Drug Development Research, Institute of Nuclear Medicine and Allied Sciences, Delhi 110054 (India); Singh, Bhawna [Department of Radiation Genetics and Epigenetics, Division of Radioprotective Drug Development Research, Institute of Nuclear Medicine and Allied Sciences, Delhi 110054 (India); Singh, Anju; Kukreti, Shrikant [Nucleic Acid Research Laboratory, Department of Chemistry, University of Delhi, Delhi 11007 (India)

2016-06-10

Highlights: • ITC study showed binding of ethyl pyruvate with BSA with high binding affinity. • Ethyl pyruvate binding caused conformation alteration of BSA. • Fluorescence quenching mechanism is static in nature. • Electrostatic, hydrogen bonding and hydrophobic forces involved in binding. • Docking confirmed role of electrostatic, hydrogen bonding and hydrophobic forces. - Abstract: Various in vitro and in vivo studies have shown the anti-inflammatory and anticancer potential role of ethyl pyruvate. Bio-distribution of drugs is significantly influenced by the drug-serum protein binding. Therefore, the binding mechanism of the ethyl pyruvate with bovine serum albumin was investigated using UV–vis absorption, fluorescence, circular dichroism, isothermal titration calorimetry and molecular docking techniques. Absorption and fluorescence quenching studies indicated the binding of ethyl pyruvate with protein. Circular dichroism spectra of bovine serum albumin confirmed significant change in the conformation of protein upon binding. Thermodynamic data confirmed that ethyl pyruvate binds to bovine serum albumin at the two different sites with high affinity. Binding of ethyl pyruvate to bovine serum albumin involves hydrogen bonding, van der Waal and hydrophobic interactions. Further, docking studies indicated that ethyl pyruvate could bind significantly at the three binding sites. The results will definitely contribute to the development of ethyl pyruvate as drug.

Changes in serum albumin conformation under the effect of UV-radiation

Energy Technology Data Exchange (ETDEWEB)

Stepuro, I I; Artsukevich, A N; Ostrovskij, Yu N [AN Belorusskoj SSR, Minsk

1981-01-01

It has been established that a rapid photolysis of one (the most libile) disulfide bridge in bull serum albumins (BSA) and man's serum albumins (MSA) is caused by the sensitizing effect of 212 and 214 triptophan residues respectively; in fact the residues decompose simultaneously with the destruction of disulfide bond. This effect is not observed in 6-8 M guanosine. Conformation rebuilding of albumin globule is observed after the destruction of disulfide bond in albumin by UV-radiation and sodium boron hydride; it is accompanied by the decrease of accessible for fluorescent probe arginine residues, the accessibility of lysine residues being unchanged. Probe fluorescent intensity - 1.8-anilinonaphthalenesulfonate - decreases after the reduction of disulfide bond by 60-70% due to the loss of accessibility for chromophore of arginine residues.

Changes in serum albumin conformation under the effect of UV-radiation

International Nuclear Information System (INIS)

Stepuro, I.I.; Artsukevich, A.N.; Ostrovskij, Yu.N.

1981-01-01

It has been established that a rapid photolysis of one (the most libile) disulfide bridge in bull serum albumins (BSA) and man's serum albumins (MSA) is caused by the sensitizing effect of 212 and 214 triptophan residues respectively; in fact the residues decompose simultaneously with the destruction of disulfide bond. This effect is not observed in 6-8 M guanosine. Conformation rebuilding of albumin globule is observed after the destruction of disulfide bond in albumin by UV-radiation and sodium boron hydride; it is accompanied by the decrease of accessible for fluorescent probe arginine residues, the accessibility of lysine residues being unchanged. Probe fluorescent intensity - 1.8-anilinonaphthalenesulfonate - decreases after the reduction of disulfide bond by 60-70% due to the loss of accessibility for chromophore of arginine residues

Interaction of Avelox with Bovine Serum Albumin and Effect of the Coexistent Drugs on the Reaction

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Baosheng Liu

2012-01-01

Full Text Available The interaction between Avelox and bovine serum albumin (BSA was investigated at different temperatures by fluorescence spectroscopy. Results showed that Avelox could quench the intrinsic fluorescence of BSA strongly, and the quenching mechanism was a static quenching process with Förester spectroscopy energy transfer. The electrostatic force played an important role on the conjugation reaction between BSA and Avelox. The order of magnitude of binding constants (Ka was 104, and the number of binding site (n in the binary system was approximately equal to 1. The binding distance (r was less than 3 nm and the primary binding site for Avelox was located in subdomain IIA of BSA. Synchronous fluorescence spectra clearly revealed that the microenvironment of amino acid residues and the conformation of BSA were changed during the binding reaction. In addition, the effect of some antibiotics on the binding constant of Avelox with BSA was also studied.

Carbonate radical anion-induced electron transfer in bovine serum albumin

Energy Technology Data Exchange (ETDEWEB)

Joshi, Ravi [Chemistry Group, Bhabha Atomic Research Centre, Mumbai 400 085 (India)]. E-mail: rjudrin@yahoo.com; Mukherjee, T. [Chemistry Group, Bhabha Atomic Research Centre, Mumbai 400 085 (India)

2006-07-15

Reaction of native and thermally denatured bovine serum albumin (BSA) with carbonate radical anion (CO{sub 3}{sup -} radical) has been studied using pulse radiolysis technique. Scavenging of CO{sub 3}{sup -} radical by native BSA and consequent electron transfer from tyrosine to tryptophan radical has been observed to occur with almost same rate constant (k{approx}1.7x10{sup 8} dm{sup 3} mol{sup -1} s{sup -1}) at pH 8.8. Effect of structural changes, due to thermal denaturation, on scavenging of CO{sub 3}{sup -} radical and the electron transfer process have been studied and discussed in this paper.

[Study of Reaction Dynamics between Bovine Serum Albumin and Folic Acid by Stopped-Flow/Fluorescence].

Science.gov (United States)

Ye, San-xian; Luo, Yun-jing; Qiao, Shu-liang; Li, Li; Liu, Cai-hong; Shi, Jian-long; An, Xue-jing

2016-01-01

As a kind of coenzyme of one-carbon enzymes in vivo, folic acid belongs to B vitamins, which can interact with other vitamins and has great significance for converting among amino acids, dividing growth of cells and protein synthesis reactions. Half-life, concentration and reaction rate constant of drugs are important parameters in pharmacokinetic study. In this paper, by utilizing fluorescence spectrophotometer and stopped-flow spectrum analyzer, reaction kinetic parameters between bovine serum albumin(BSA) and folic acid in a bionic system have been investigated, which provide references for parameters of drug metabolism related to folic acid. By using Stern-Volmer equation dealing with fluorescence quenching experiments data, we concluded that under 25, 30, and 37 degrees C, the static quenching constants of folic acid to intrinsic fluorescence from bovine serum albumin were 2.455 x 10(10), 4.900 x 10(10) and 6.427 x 10(10) L x mol(-1) x s(-1) respectively; The results of kinetic reaction rate have shown that the reaction rate of BSA and folic acid are greater than 100 mol x L(-1) x s(-1) at different temperatures, pH and buffering media, illustrating that the quenching mechanism between BSA and folic acid is to form composite static quenching process. Reaction concentration of bovine serum albumin and its initial concentration were equal to the secondary reaction formula, and the correlation coefficient was 0.998 7, while the half-life (t1/2) was 0.059 s at physiological temperature. With the increase of folic acid concentration, the apparent rate constant of this reaction had a linear increasing trend, the BSA fluorescence quenching rate constant catalyzed by folic acid was 3.174 x 10(5) mol x L(-1) x s(-1). Furthermore, with different buffer, the apparent rate constant and reaction rate constant of BSA interacting with folic acid were detected to explore the influence on the reaction under physiological medium, which is of great significance to determine the

Determination of Conjugation Efficiency of Antibodies and Proteins to the Superparamagnetic Iron Oxide Nanoparticles by Capillary Electrophoresis with Laser-Induced Fluorescence Detection

Energy Technology Data Exchange (ETDEWEB)

Wang, F.-H.; Yoshitake, Takashi [Karolinska Institutet, Department of Neuroscience (Sweden); Kim, Do-Kyung; Muhammed, Mamoun [Royal Institute of Technology, Materials Chemistry Division (Sweden); Bjelke, Boerje [MRI-Center, Experimental Unit, Karolinska Institutet (Sweden); Kehr, Jan [Karolinska Institutet, Department of Neuroscience (Sweden)], E-mail: Jan.Kehr@neuro.ki.se

2003-04-15

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.

Study of Interaction between Cadmium and Bovine Serum Albumin with UV-Vis Spectrocopy Approach

Science.gov (United States)

Suhartono, E.; Thalib, I.; Aflanie, I.; Noor, Z.; Idroes, R.

2018-05-01

This study aims to explain the interaction of cadmium (Cd) with serum albumin through visible light (UV-Vis) spectroscopy approach. This study is an in vitro experimental study using Cd with several concentrations and Bovine Serum Albumin (BSA). Each solution was then incubated for 10 min at 37°C, and measured the absorbance at 220-300 nm. The absorbance data is then presented in graphical form. From the graph, a linear equation will appear to calculate the value of metal binding constants (K) to proteins. Also, in this present study we analsyed the ratio between A220 and A220 to identify changes in the protein region especially tyrosine and peptide bonds. The results show that the addition of Cd in different concentrations could increase the absorbance with a constant value (K) = 1.634. Based on the result, it seems the addition of Cd in different concentrations will lead the reaction to form BSA-Cd. Also, the result shows that the ration of A220/A280 were decreased with the increasing of Cd concentration. In conclusion, the addition of Cd could interact and changes the protein structure in BSA.

Biological Interaction of Molybdenocene Dichloride with Bovine Serum Albumin Using Fluorescence Spectroscopy

Science.gov (United States)

Domínguez, Moralba; Cortes-Figueroa, Jose´ E.; Meléndez, Enrique

2018-01-01

Bioinorganic topics are ubiquitous in the inorganic chemistry curriculum; however, experiments to enhance understanding of related topics are scarce. In this proposed laboratory, upper undergraduate students assess the biological interaction of molybdenocene dichloride (Cp2MoCl2) with bovine serum albumin (BSA) by fluorescence spectroscopy.…

Bovine serum albumin bioconjugated graphene oxide: Red blood cell adhesion and hemolysis studied by QCM-D

Science.gov (United States)

Cai, Bing; Hu, Kebang; Li, Chunming; Jin, Jing; Hu, Yuexin

2015-11-01

Graphene oxide (GO) had great potential in various applications especial biomedical materials. In this study, we improved the hemocompatibility especial hemolysis properties of GO nanosheets by grafting bovine serum albumin (BSA). The hemocompatibility of GO-g-BSA was improved. The hemolysis ratio of GO-g-BSA was lower than 0.2% and no visible hemoglobin release was observed. In a flowed condition, the interaction between GO and RBC was monitored real time by quartz crystal microbalance with dissipation (QCM-D) and the hemolysis rates of eluted RBC solution was determined. The balance between the adsorption and degradation of RBC on the surface of GO was a linear process. The GO-g-BSA surface decreased the adhesion of RBC in a flowed condition, maintained the morphology of RBC and reduced the hemolysis rate in the most effective manner. The inert of BSA resisted GO interacting with the lipid bilayers of RBC and the negative charge on the surface of BSA repelled the approach of negative charged RBC. The excellent hemocompatibility of the BSA modified GO might confer its great potentials for various biomedical applications.

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.

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.

Binding thermodynamics of Diclofenac and Naproxen with human and bovine serum albumins: A calorimetric and spectroscopic study

International Nuclear Information System (INIS)

Bou-Abdallah, Fadi; Sprague, Samuel E.; Smith, Britannia M.; Giffune, Thomas R.

2016-01-01

Highlights: • The binding affinity of Diclofenac and Naproxen to BSA and HSA is on the order of 10 4 –10 6 M −1 . • Two Diclofenac molecules bind per BSA or HSA but only 0.75 and 3 Naproxen molecules bind to BSA and HSA, respectively. • Drugs binding to BSA is only enthalpically favored and both enthalpically and entropically favored for HSA. • Fluorescence quenching data suggest dynamic collisions and the formation of ground-state protein-drug complexes. • DSC data show multiple sequential unfolding events and strong drug stabilization effects. - Abstract: Serum albumins are ubiquitous proteins able to bind a variety of exogenous and endogenous ligands including hydrophobic pharmaceuticals. Most drugs bind to two very active binding regions located within sub-domains IIA and IIIA of the protein, also known as Sudlow’s sites. The drug binding mode of serum albumin provides important pharmacological information and influences drug solubility, efficacy, biological distribution, and excretion. Here, the binding thermodynamics of Diclofenac and Naproxen, two non-steroidal anti-inflammatory drugs (NSAIDs) to bovine and human serum albumins (BSA and HSA, respectively) were studied by isothermal titration calorimetry (ITC), fluorescence spectroscopy and differential scanning calorimetry (DSC). The ITC data show that the binding affinity (K) of Diclofenac to BSA and HSA is on the order of 10 4 M −1 with a binding stoichiometry (n) of 2 drug molecules per protein. Naproxen binding to the two proteins exhibits a different profile with K and n values on the order of 10 6 M −1 and 0.75 for BSA, and 10 5 M −1 and 3 for HSA, respectively. The binding of the two drugs to HSA is found to be both enthalpically and entropically favored suggesting the formation of hydrogen bonds and van der Waals hydrophobic effects. Binding of the two drugs to BSA is only enthalpically favored with an unfavorable entropy term. Significant enthalpy–entropy compensation

Molecular binding of toxic phenothiazinium derivatives, azures to bovine serum albumin: A comparative spectroscopic, calorimetric, and in silico study.

Science.gov (United States)

Das, Somnath; Islam, Md Maidul; Jana, Gopal Chandra; Patra, Anirudha; Jha, Pradeep K; Hossain, Maidul

2017-07-01

In this paper, the comparative binding behavior of antimalarial drug azure A, azure B and azure C with bovine serum albumin (BSA) has been studied. The interaction has been confirmed by multispectroscopic (UV, fluorescence, Fourier transform infrared (FT-IR), and circular dichroism) and molecular docking techniques. The experimental results show that azure B has the highest BSA binding affinity followed by azure A and azure C. The experimental evidence of binding showed a static quenching mechanism in the interaction azures with BSA. The isothermal titration calorimetry result reveals that the binding was exothermic with positive entropy contribution in each case. The thermodynamic parameters ΔH, ΔG, and ΔS at 25°C were calculated, which indicates that the weak van der Waals forces and hydrogen bonding rather than the hydrophobic effect played an important role in the interaction. According to the theory of Förster nonradiative energy transfer, the distance (r) between the donor (BSA) and acceptor azures found to be albumins. We hope, the outcome of this work will be most helpful for synthesizing a new type of phenothiazinium derivatives of the better therapeutic application. Copyright © 2017 John Wiley & Sons, Ltd.

Fluorescent bovine serum albumin interacting with the antitussive quencher dextromethorphan: a spectroscopic insight.

Science.gov (United States)

Durgannavar, Amar K; Patgar, Manjanath B; Nandibewoor, Sharanappa T; Chimatadar, Shivamurti A

2016-05-01

The interaction of dextromethorphan hydrobromide (DXM) with bovine serum albumin (BSA) is studied by using fluorescence spectra, UV-vis absorption, synchronous fluorescence spectra (SFS), 3D fluorescence spectra, Fourier transform infrared (FTIR) spectroscopy and circular dichroism under simulated physiological conditions. DXM effectively quenched the intrinsic fluorescence of BSA. Values of the binding constant, K(A), are 7.159 × 10(3), 9.398 × 10(3) and 16.101 × 10(3)  L/mol; the number of binding sites, n, and the corresponding thermodynamic parameters ΔG°, ΔH° and ΔS° between DXM and BSA were calculated at different temperatures. The interaction between DXM and BSA occurs through dynamic quenching and the effect of DXM on the conformation of BSA was analyzed using SFS. The average binding distance, r, between the donor (BSA) and acceptor (DXM) was determined based on Förster's theory. The results of fluorescence spectra, UV-vis absorption spectra and SFS show that the secondary structure of the protein has been changed in the presence of DXM. Copyright © 2015 John Wiley & Sons, Ltd.

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. Copyright © 2015 John Wiley & Sons, Ltd.

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

Thermodynamic studies on the interaction of folic acid with bovine serum albumin

International Nuclear Information System (INIS)

Jha, Niki S.; Kishore, Nand

2011-01-01

Research highlights: → Thermodynamics of binding of folic acid with bovine serum albumin studied. → Effect of co-solutes on binding permitted detailed analysis of interactions. → Electrostatic interactions dominate with contribution from hydrogen bonding. → No significant conformational change in protein observed upon drug binding. - Abstract: Binding of the vitamin folic acid with bovine serum albumin (BSA) has been studied using isothermal titration calorimetry (ITC) in combination with fluorescence and circular dichroism spectroscopies. The thermodynamic parameters of binding have been evaluated as a function of temperature, ionic strength, in the presence of nonionic surfactants triton X-100, tetrabutylammonium bromide, and sucrose. The values of the van't Hoff enthalpy calculated from the temperature dependence of the binding constant agree with the calorimetric enthalpies indicating that the binding of folic acid to the BSA is a two state process without involving intermediates. These observations are supported by the intrinsic fluorescence and circular dichroism spectroscopic measurements. With increase in the ionic strength, reduction in the binding affinity of folic acid to BSA is observed suggesting predominance of electrostatic interactions in the binding. The contribution of hydrophobic interactions in the binding is also demonstrated by decrease in the binding affinity in the presence of tetrabutylammonium bromide (TBAB). The value of binding affinity in the presence of sucrose indicates that hydrogen bonding also plays a significant contribution in the complexation process. The calorimetric and spectroscopic results provide quantitative information on the binding of folic acid to BSA and suggest that the binding is dominated by electrostatic interactions with contribution from hydrogen bonding.

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.

Kinetics of the Adsorption of Bovine Serum Albumin of White Wine ...

African Journals Online (AJOL)

This study investigates the kinetics of adsorption of bovine serum albumin, BSA, in white wine model solutions onto activated carbon, AC, and alumina, AL. Pseudo-first order and pseudo-second order models were applied to determine the rate and mechanism of adsorption of the white wine protein during the haze removal ...

Synthetic surfactant- and cross-linker-free preparation of highly stable lipid-polymer hybrid nanoparticles as potential oral delivery vehicles.

Science.gov (United States)

Wang, Taoran; Xue, Jingyi; Hu, Qiaobin; Zhou, Mingyong; Chang, Chao; Luo, Yangchao

2017-06-05

The toxicity associated with concentrated synthetic surfactants and the poor stability at gastrointestinal condition are two major constraints for practical applications of solid lipid nanoparticles (SLN) as oral delivery vehicles. In this study, a synthetic surfactant-free and cross-linker-free method was developed to fabricate effective, safe, and ultra-stable lipid-polymer hybrid nanoparticles (LPN). Bovine serum albumin (BSA) and dextran varying in molecular weights were first conjugated through Maillard reaction and the conjugates were exploited to emulsify solid lipid by a solvent diffusion and sonication method. The multilayer structure was formed by self-assembly of BSA-dextran micelles to envelope solid lipid via a pH- and heating-induced facile process with simultaneous surface deposition of pectin. The efficiency of different BSA-dextran conjugates was systematically studied to prepare LPN with the smallest size, the most homogeneous distribution and the greatest stability. The molecular interactions were characterized by Fourier transform infrared and fluorescence spectroscopies. Both nano spray drying and freeze-drying methods were tested to produce spherical and uniform pectin-coated LPN powders that were able to re-assemble nanoscale structure when redispersed in water. The results demonstrated the promise of a synthetic surfactant- and cross-linker-free technique to prepare highly stable pectin-coated LPN from all natural biomaterials as potential oral delivery vehicles.

Comparative Studies on the Interaction of Cochinchinenin A and Loureirin B with Bovine Serum Albumin

Directory of Open Access Journals (Sweden)

Tianming Yang

2013-01-01

Full Text Available This paper describes the simple, sensitive, and effective spectrophotometric methods based on ultraviolet, fluorescence and circular dichroism for revealing the interactional mechanism of Cochinchinenin A (CA and Loureirin B (LB with bovine serum albumin (BSA. Under simulated physiological conditions, it was demonstrated that the fluorescence quenching mechanisms between CA (or LB and BSA as a static quenching mode, or a combined quenching (dynamic and static quenching mode were related to concentration level of CA (or LB. The binding distance (rCA, rLB and the quenching efficiency (KSV, especially for the binding constants value of ligands to BSA, were affected by the methoxyl group at position 4 at different temperatures. The corresponding thermodynamic parameters were also obtained and indicated that electrostatic forces play a major role in the formation of the LB-BSA complex, but probably a combined force for CA-BSA complex. Furthermore, synchronous fluorescence spectroscopy and circular dichroism spectra demonstrated that the secondary structures of BSA were changed to varying degrees by the binding of CA (or LB.

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 tertiary carbon-centred radicals and disruption of the tryptophan ring system. In the case of porphyrins such as hematoporphyrin, which bind at specific sites on BSA, these species appear to arise via long-range transfer of damage within the protein structure, as the binding site is some distance from...... the ultimate site of radical formation. This transfer of damage is shown to depend on a number of factors including the conformation of the protein, the presence of blocking groups and pH. Alteration of the protein conformation results in radical formation at additional (or alternative) sites, as does blocking...

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...... 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 mediate its transport...

Fabrication and Assessment of ZnO Modified Polyethersulfone Membranes for Fouling Reduction of Bovine Serum Albumin

Directory of Open Access Journals (Sweden)

Tshepo Duncan Dipheko

2017-01-01

Full Text Available ZnO/PES composite membranes were fabricated by phase inversion method using DMAc as a solvent. The structure of ZnO was investigated using TEM, SEM, XRD, and TGA. TEM images of ZnO nanoparticles were well-defined, small, and spherically shaped with agglomerated nanoparticles particles of 50 nm. The SEM and XRD results were an indication that ZnO nanoparticles were present in the prepared ZnO/PES composites membranes. Contact angle measurements were used to investigate surface structures of the composite membranes. The amount of ZnO nanoparticles on PES membranes was varied to obtain the optimal performance of the composite membranes in terms of pure water flux, flux recovery, and fouling resistance using the protein bovine serum albumin (BSA as a model organic foulant. The results showed that addition of ZnO to PES membranes improved the hydrophilicity, permeation, and fouling resistance properties of the membranes. Pure water flux increased from a low of 250 L/m2h for the neat membrane to a high of 410 L/m2h for the composite membranes. A high flux recovery of 80–94% was obtained for the composite membranes. The optimal performance of the composite membranes was obtained at 1.5 wt% of ZnO.

Study of Interactions of an Anticancer Drug Neratinib With Bovine Serum Albumin: Spectroscopic and Molecular Docking Approach

OpenAIRE

Tanveer A. Wani; Ahmed H. Bakheit; Ahmed H. Bakheit; M. A. Abounassif; Seema Zargar

2018-01-01

Binding of therapeutic agents to plasma proteins, particularly to serum albumin, provides valuable information in the drug development. This study was designed to evaluate the binding interaction of neratinib with bovine serum albumin (BSA). Neratinib blocks HER2 signaling and is effective in trastuzumab-resistant breast cancer treatment. Spectrofluorometric, UV spectrophotometric, and fourier transform infrared (FT-IR) and molecular docking experiments were performed to study this interactio...

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.

Enhanced tumor targeting of cRGD peptide-conjugated albumin nanoparticles in the BxPC-3 cell line.

Science.gov (United States)

Yu, Xinzhe; Song, Yunlong; Di, Yang; He, Hang; Fu, Deliang; Jin, Chen

2016-08-12

The emerging albumin nanoparticle brings new hope for the delivery of antitumor drugs. However, a lack of robust tumor targeting greatly limits its application. In this paper, cyclic arginine-glycine-aspartic-conjugated, gemcitabine-loaded human serum albumin nanoparticles (cRGD-Gem-HSA-NPs) were successfully prepared, characterized, and tested in vitro in the BxPC-3 cell line. Initially, 4-N-myristoyl-gemcitabine (Gem-C14) was formed by conjugating myristoyl to the 4-amino group of gemcitabine. Then, cRGD-HSA was synthesized using sulfosuccinimidyl-(4-N-maleimidomethyl)cyclohexane-1-carboxylate (Sulfo-SMCC) cross-linkers. Finally, cRGD-Gem-HSA-NPs were formulated based on the nanoparticle albumin-bound (nab) technology. The resulting NPs were characterized for particle size, zeta potential, morphology, encapsulation efficiency, and drug loading efficiency. In vitro cellular uptake and inhibition studies were conducted to compare Gem-HSA-NPs and cRGD-Gem-HSA-NPs in a human pancreatic cancer cell line (BxPC-3). The cRGD-Gem-HSA-NPs exhibited an average particle size of 160 ± 23 nm. The encapsulation rate and drug loading rate were approximately 83 ± 5.6% and 11 ± 4.2%, respectively. In vitro, the cRGD-anchored NPs exhibited a significantly greater affinity for the BxPC-3 cells compared to non-targeted NPs and free drug. The cRGD-Gem-HSA-NPs also showed the strongest inhibitory effect in the BxPC-3 cells among all the analyzed groups. The improved efficacy of cRGD-Gem-HSA-NPs in the BxPC-3 cell line warrants further in vivo investigations.

Dry powder pulmonary delivery of cationic PGA-co-PDL nanoparticles with surface adsorbed model protein.

Science.gov (United States)

Kunda, Nitesh K; Alfagih, Iman M; Dennison, Sarah R; Somavarapu, Satyanarayana; Merchant, Zahra; Hutcheon, Gillian A; Saleem, Imran Y

2015-08-15

Pulmonary delivery of macromolecules has been the focus of attention as an alternate route of delivery with benefits such as; large surface area, thin alveolar epithelium, rapid absorption and extensive vasculature. In this study, a model protein, bovine serum albumin (BSA) was adsorbed onto cationic PGA-co-PDL polymeric nanoparticles (NPs) prepared by a single emulsion solvent evaporation method using a cationic surfactant didodecyldimethylammonium bromide (DMAB) at 2% w/w (particle size: 128.64±06.01 nm and zeta-potential: +42.32±02.70 mV). The optimum cationic NPs were then surface adsorbed with BSA, NP:BSA (100:4) ratio yielded 10.01±1.19 μg of BSA per mg of NPs. The BSA adsorbed NPs (5 mg/ml) were then spray-dried in an aqueous suspension of L-leucine (7.5 mg/ml, corresponding to a ratio of 1:1.5/NP:L-leu) using a Büchi-290 mini-spray dryer to produce nanocomposite microparticles (NCMPs) containing cationic NPs. The aerosol properties showed a fine particle fraction (FPF, dae<4.46 μm) of 70.67±4.07% and mass median aerodynamic diameter (MMAD) of 2.80±0.21 μm suggesting a deposition in the respiratory bronchiolar region of the lungs.The cell viability was 75.76±03.55% (A549 cell line) at 156.25 μg/ml concentration after 24 h exposure. SDS-PAGE and circular dichroism (CD) confirmed that the primary and secondary structure of the released BSA was maintained. Moreover, the released BSA showed 78.76±1.54% relative esterolytic activity compared to standard BSA. Copyright © 2015 Elsevier B.V. All rights reserved.

Modeling water partition in composite gels of BSA with gelatin following high pressure treatment.

Science.gov (United States)

Semasaka, Carine; Mhaske, Pranita; Buckow, Roman; Kasapis, Stefan

2018-11-01

Changes in the structural properties of hydrogels made with gelatin and bovine serum albumin mixtures were recorded following exposure to high pressure at 300 MPa for 15 min at 10 and 80 °C. Dynamic oscillation, SEM, FTIR and blending law modelling were utilised to rationalise results. Pressurization at the low temperature end yielded continuous gelatin networks supporting discontinuous BSA inclusions, whereas an inverted dispersion was formed at the high temperature end with the continuous BSA network suspending the discontinuous gelatin inclusions. Lewis and Nielsen equations followed the mechanical properties of the composites thus arguing that solvent partition between the two phases was always in favour of the polymer forming the continuous network. As far as we are aware, this is the first attempt to elucidate the solvent partition in pressurised hydrogel composites using blending law theory. Outcomes were contrasted with earlier work where binary mixtures were subjected only to thermal treatment. Copyright © 2018. Published by Elsevier Ltd.

The investigation of the interaction between edaravone and bovine serum albumin by spectroscopic approaches

International Nuclear Information System (INIS)

Yu Xianyong; Yang Ying; Liu Ronghua; Huang Haowen; Chen Jian; Ji Danhong; Li Xiaofang; Yang Fengxian; Yi Pinggui

2011-01-01

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 (ΔG, ΔH, and ΔS) 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 2+ , Ca 2+ , Cu 2+ , and Ni 2+ on the binding constant between EDA and BSA were examined. - Highlights: → We explored the interaction of BSA and EDA using spectroscopic methods. → The fluorescence quenching mechanism is combined quenching. → Hydrophobic interaction force plays a major role in stabilizing the complex. → The binding constants, binding sites, and thermodynamic parameters were calculated. → EDA affects the conformation of tryptophan residue's microregion.

The investigation of the interaction between edaravone and bovine serum albumin by spectroscopic approaches

Energy Technology Data Exchange (ETDEWEB)

Xianyong, Yu; Ying, Yang; Ronghua, Liu; Haowen, Huang; Jian, Chen; Danhong, Ji [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); Fengxian, Yang [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.

Study on the conformal variations of bovine and human serum albumin in solution using small angle X-ray scattering

International Nuclear Information System (INIS)

Olivieri, Johnny Rizzieri.

1992-01-01

It is reported a Small Angle X-Ray Scattering (SAXS) study of BSA (Bovine Serum Albumin) and HSA (Human Serum Albumin) on pH between 2.5 and 7.0. The measured scattering intensities, normalized in relation to incident beam, exposition time and scattering due to solvent and capillary, and corrected due to concentration and beam shape effects, have shown a strong dependence of the protein shape with pH for both albumins. It was found that the radius of gyration varies between 26.7 and 35 A, and the analyses of the distance distribution function. P(r), indicated that these proteins undergoes conformational changes with pH. Different theoretical shapes have been proposed and analysed comparing the computed P(r) function generated from the models with the experimental P(r). A large variety of shapes were found in both proteins, indicating that BSA and HSA are very flexibility macromolecules. (author). 60 refs., 49 figs., 7 tabs

Effect of calcium, bicarbonate, and albumin on capacitation-related events in equine sperm.

Science.gov (United States)

Macías-García, B; González-Fernández, L; Loux, S C; Rocha, A M; Guimarães, T; Peña, F J; Varner, D D; Hinrichs, K

2015-01-01

Repeatable methods for IVF have not been established in the horse, reflecting the failure of standard capacitating media to induce changes required for fertilization capacity in equine sperm. One important step in capacitation is membrane cholesterol efflux, which in other species is triggered by cholesterol oxidation and is typically enhanced using albumin as a sterol acceptor. We incubated equine sperm in the presence of calcium, BSA, and bicarbonate, alone or in combination. Bicarbonate induced an increase in reactive oxygen species (ROS) that was abolished by the addition of calcium or BSA. Bicarbonate induced protein tyrosine phosphorylation (PY), even in the presence of calcium or BSA. Incubation at high pH enhanced PY but did not increase ROS production. Notably, no combination of these factors was associated with significant cholesterol efflux, as assessed by fluorescent quantitative cholesterol assay and confirmed by filipin staining. By contrast, sperm treated with methyl-β-cyclodextrin showed a significant reduction in cholesterol levels, but no significant increase in PY or ROS. Presence of BSA increased sperm binding to bovine zonae pellucidae in all three stallions. These results show that presence of serum albumin is not associated with a reduction in membrane cholesterol levels in equine sperm, highlighting the failure of equine sperm to exhibit core capacitation-related changes in a standard capacitating medium. These data indicate an atypical relationship among cholesterol efflux, ROS production, and PY in equine sperm. Our findings may help to elucidate factors affecting failure of equine IVF under standard conditions. © 2015 Society for Reproduction and Fertility.

Interactions of hemin with bovine serum albumin and human hemoglobin: A fluorescence quenching study

Science.gov (United States)

Makarska-Bialokoz, Magdalena

2018-03-01

The binding interactions between hemin (Hmi) and bovine serum albumin (BSA) or human hemoglobin (HHb), respectively, have been examined in aqueous solution at pH = 7.4, applying UV-vis absorption, as well as steady-state, synchronous and three-dimensional fluorescence spectra techniques. Representative results received for both BSA and HHb intrinsic fluorescence proceeding from the interactions with hemin suggest the formation of stacking non-covalent and non-fluorescent complexes in both the Hmi-BSA and Hmi-HHb systems, with highly possible concurrent formation of a coordinate bond between a group on the protein surface and the metal in Hmi molecule. All the values of calculated parameters, the binding, fluorescence quenching and bimolecular quenching rate constants point to the involvement of static quenching in both the systems studied. The blue shift in the synchronous fluorescence spectra imply the participation of both tryptophan and tyrosine residues in quenching of BSA and HHb intrinsic fluorescence. Depicted outcomes suggest that hemin is supposedly able to influence the physiological functions of BSA and HHb, the most important blood proteins, particularly in case of its overuse.

Graphdiyne Nanoparticles with High Free Radical Scavenging Activity for Radiation Protection.

Science.gov (United States)

Xie, Jiani; Wang, Ning; Dong, Xinghua; Wang, Chengyan; Du, Zhen; Mei, Linqiang; Yong, Yuan; Huang, Changshui; Li, Yuliang; Gu, Zhanjun; Zhao, Yuliang

2018-03-06

Numerous carbon networks materials comprised of benzene moieties, such as graphene and fullerene, have held great fascination for radioprotection because of their acknowledged good biocompatibility and strong free radical scavenging activity derived from their delocalized π-conjugated structure. Recently, graphdiyne, a new emerging carbon network material consisting of a unique chemical structure of benzene and acetylenic moieties, has gradually attracted attention in many research fields. Encouraged by its unique structure with strong conjugated π-system and highly reactive diacetylenic linkages, graphdiyne might have free radical activity and can thus be used as a radioprotector, which has not been investigated so far. Herein, for the first time, we synthesized bovine serum albumin (BSA)-modified graphdiyne nanoparticles (graphdiyne-BSA NPs) to evaluate their free radical scavenging ability and investigate their application for radioprotection both in cell and animal models. In vitro studies indicated that the graphdiyne-BSA NPs could effectively eliminate the free-radicals, decrease radiation-induced DNA damage in cells, and improve the viability of cells under ionizing radiation. In vivo experiments showed that the graphdiyne-BSA NPs could protect the bone marrow DNA of mice from radiation-induced damage and make the superoxide dismutase (SOD) and malondialdehyde (MDA) (two kinds of vital indicators of radiation-induced injury) recover back to normal levels. Furthermore, the good biocompatibility and negligible systemically toxicity responses of the graphdiyne-BSA NPs to mice were verified. All these results manifest the good biosafety and radioprotection activity of graphdiyne-BSA NPs to normal tissues. Therefore, our studies not only provide a new radiation protection platform based on graphdiyne for protecting normal tissues from radiation-caused injury but also provide a promising direction for the application of graphdiyne in the biomedicine field.

Competitive adsorption of albumin and monoclonal immuno upsilon globulin molecules on polystyrene surfaces

NARCIS (Netherlands)

Elgersma, F.

1990-01-01

The subject of this thesis is proteins at interfaces. The main purpose of the work was to acquire more insight into the mechanism of adsorption of Bovine Serum Albumin (BSA) and monoclonal Immuno gamma Globulins (IgG's). both individually and in competition. Another aim was to achieve

Novel thermo-sensitive core-shell nanoparticles for targeted paclitaxel delivery

International Nuclear Information System (INIS)

Li Yuanpei; Pan Shirong; Zhang Wei; Du Zhuo

2009-01-01

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.

Biomolecule-coated metal nanoparticles on titanium.

Science.gov (United States)

Christensen, Stephen L; Chatt, Amares; Zhang, Peng

2012-02-07

Immobilizations of nanoparticles and biomolecules on biocompatible substrates such as titanium are two promising approaches to bringing new functionalities to Ti-based biomaterials. Herein, we used a variety of X-ray spectroscopic techniques to study and better understand metal-thiolate interactions in biofunctionalized metal nanoparticle systems supported on Ti substrates. Using a facile one-step procedure, a series of Au nanoparticle samples with varied biomolecule coatings ((2-mercatopropionyl)glycine (MPG) and bovine serum albumin (BSA)) and biomolecule concentrations are prepared. Ag and Pd systems are also studied to observe change with varying metal composition. The structure and properties of these biomolecule-coated nanoparticles are investigated with scanning electron microscopy (SEM) and element-specific X-ray techniques, including extended X-ray absorption fine structure (Au L(3)-edge), X-ray absorption near-edge structure (Au L(3), Ag L(3), Pd L(3), and S K-edge), and X-ray photoelectron spectroscopy (Au 4f, Ag 3d, Pd 3d, and S 2p core level). It was found that, by comparison of SEM and X-ray spectroscopy results, the coating of metal nanoparticles with varying model biomolecule systems can have a significant effect on both surface coverage and organization. This work offers a facile chemical method for bio- and nanofunctionalization of Ti substrates as well as provides a physical picture of the structure and bonding of biocoated metal nanoparticles, which may lead to useful applications in orthopedics and biomedicine.

Study on interaction of Ligupurpuroside A with bovine serum albumin by multi-spectroscopic methods

Energy Technology Data Exchange (ETDEWEB)

Shen, Liang-liang [College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen 518060 (China); Xu, Hong, E-mail: xuhong@szu.edu.cn [College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen 518060 (China); Huang, Feng-wen; Li, Yi; Xiao, Jie; Xiao, Hua-feng; Ying, Ming; Tian, Sheng-li; Yang, Zhen; Liu, Gang; Hu, Zhang-li [College of Life Sciences, Shenzhen Key Laboratory of Marine Bioresources and Ecology/Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen 518060 (China); He, Zhen-dan, E-mail: hezhendan@126.com [School of Medicine, Shenzhen University, Shenzhen 518060 (China); Zhou, Kai [Shenzhen Marine Environment and Resource Monitoring Center, Shenzhen 518060 (China)

2014-10-15

The interaction of Ligupurpuroside A with bovine serum albumin (BSA) has been investigated by fluorescence spectra, UV–vis absorption spectra, three-dimensional (3D) fluorescence spectra, synchronous fluorescence spectra and circular dichroism (CD) spectra along with a molecular docking method. The fluorescence experiments indicate that Ligupurpuroside A can quench the intrinsic fluorescence of BSA through a combined quenching way at the low concentration of Ligupurpuroside A, and a static quenching procedure at the high concentration. The thermodynamic analysis suggests that hydrogen bonds and van der Waals forces are the main forces between BSA and Ligupurpuroside A. According to the theory of Förster's non-radiation energy transfer, the binding distance between BSA and Ligupurpuroside A was calculated to be 2.73 nm, which implies that energy transfer occurs between BSA and Ligupurpuroside A. All these experimental results have been validated by the protein–ligand docking studies which show that Ligupurpuroside A binds to the residues located in the hydrophobic cavity on subdomain IIA of BSA. In addition, conformation change of BSA was observed from three-dimensional fluorescence spectra, synchronous fluorescence spectra and circular dichroism spectra under experimental conditions. - Highlights: • The interaction of Ligupurpuroside A with BSA was investigated. • The fluorescence quenching of BSA induced by Ligupurpuroside A is a combined quenching process. • The main interaction forces were hydrogen bonds and van der Waals forces. • Ligupurpuroside A binding results in a decrease in α-helix.

Interaction of different thiol-capped CdTe quantum dots with bovine serum albumin

International Nuclear Information System (INIS)

Wang Qisui; Zhang Xiaolei; Zhou Xiaolan; Fang Tingting; Liu Pengfei; Liu Peng; Min Xinmin; Li, Xi

2012-01-01

Due to their unique optical properties, quantum dots (QDs) are rapidly revolutionizing many areas of medicine and biology. Despite the remarkable speed of development of nanoscience, relatively little is known about the interaction of nanoscale objects with organism. In this work, interaction of CdTe QDs coated with mercaptopropanoic acid (MPA), L-cysteine (L-cys), and glutathione (GSH) with bovine serum albumin (BSA) was investigated. Fluorescence (FL), UV–vis absorption, and circular dichroism (CD) spectra methods were used. The Stern-Volmer quenching constant (K sv ) at different temperatures, corresponding thermodynamic parameters (ΔH, ΔG and ΔS), and information of the structural features of BSA were gained. We found that QDs can effectively quench the FL of BSA in a ligand-dependent manner, electrostatic interactions play a major role in the binding reaction, and the nature of quenching is static, resulting in forming QDs-BSA complexes. The CD spectra showed that the secondary and tertiary structure of BSA was changed. This study contributes to a better understanding of the ligand effects on QDs-proteins interactions, which is a critical issue for the applications in vivo. - Highlights: ► The interaction between three thiol-capped QDs and BSA by UV–vis, FL, and CD spectra. ► The bio-effect of CdTe QDs on BSA was a ligand-dependent manner. ► The thermodynamic parameters and the structural features of BSA were gained.

Adsorption behavior of cation-exchange resin-mixed polyethersulfone-based fibrous adsorbents with bovine serum albumin

NARCIS (Netherlands)

Zhang, Y.; Zhang, Yuzhong; Borneman, Zandrie; Koops, G.H.; Wessling, Matthias

2006-01-01

The cation-exchange resin-mixed polyethersulfone (PES)-based fibrous adsorbents were developed to study their adsorption behavior with bovine serum albumin (BSA). A fibrous adsorbent with an open pore surface had much better adsorption behavior with a higher adsorbing rate. The adsorption capacity

Fabrication and characterization of SPR chips with the modified bovine serum albumin

Science.gov (United States)

Chen, Xing; Zhang, Lu-lu; Cui, Da-fu

2016-03-01

A facile surface plasmon resonance (SPR) chip is developed for small molecule determination and analysis. The SPR chip was prepared based on a self assembling principle, in which the modified bovine serum albumin (BSA) was directly self-assembled onto the bare gold surface. The surface morphology of the chip with the modified BSA was investigated by atomic force microscopy (AFM) and its optical properties were characterized. The surface binding capacity of the bare facile SPR chip with a uniform morphology is 8 times of that of the bare control SPR chip. Based on the experiments of immune reaction between cortisol antibody and cortisol derivative, the sensitivity of the facile SPR chip with the modified BSA is much higher than that of the control SPR chip with the un-modified BSA. The facile SPR chip has been successfully used to detect small molecules. The lowest detection limit is 5 ng/mL with a linear range of 5—100 ng/mL for cortisol analysis. The novel facile SPR chip can also be applied to detect other small molecules.

Microwave-assisted synthesis of L-glutathione capped ZnSe QDs and its interaction with BSA by spectroscopy

Energy Technology Data Exchange (ETDEWEB)

Ding, Ling, E-mail: linda0911@163.com [College of Chemical Engineering and Technology, Wuhan University of Science and Technology, Wuhan 430081 (China); College of Resource and Environmental Sciences, Hubei Biomass-Resource Chemistry and Environmental Biotechnology Key Laboratory, Wuhan University, Wuhan 430079 (China); Zhou, Pei-Jiang, E-mail: zhoupj@whu.edu.cn [College of Resource and Environmental Sciences, Hubei Biomass-Resource Chemistry and Environmental Biotechnology Key Laboratory, Wuhan University, Wuhan 430079 (China); Zhan, Hong-Ju [College of Resource and Environmental Sciences, Hubei Biomass-Resource Chemistry and Environmental Biotechnology Key Laboratory, Wuhan University, Wuhan 430079 (China); Jingchu University of Technology, Jingmen 448000 (China); Chen, Chi [College of Resource and Environmental Sciences, Hubei Biomass-Resource Chemistry and Environmental Biotechnology Key Laboratory, Wuhan University, Wuhan 430079 (China); Hu, Wei [Wuhan Humanwell Pharmaceutical Co. Ltd, Wuhan 430064 (China); Zhou, Teng-Fei; Lin, Chao-Wang [College of Resource and Environmental Sciences, Hubei Biomass-Resource Chemistry and Environmental Biotechnology Key Laboratory, Wuhan University, Wuhan 430079 (China)

2013-10-15

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.

Investigation of three flavonoids binding to bovine serum albumin using molecular fluorescence technique

International Nuclear Information System (INIS)

Bi Shuyun; Yan Lili; Pang Bo; Wang Yu

2012-01-01

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 A n aringenin) =4.08x10 4 A(hesperetin) =5.40x10 4 ∼K A(apigenin) =5.32x10 4 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 (r 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 3+ , Cu 2+ , Mg 2+ , Mn 2+ , Zn 2+ and Ca 2+ 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.

Enhanced bovine serum albumin absorption on the N-hydroxysuccinimide activated graphene oxide and its corresponding cell affinity.

Science.gov (United States)

Xiong, Kun; Fan, Qingbo; Wu, Tingting; Shi, Haishan; Chen, Lin; Yan, Minhao

2017-12-01

By successively reacting with N-(3-Dimethylaminopropyl)-N'-ethylcarbodiimide hydrochloride (EDC) and N-hydroxysuccinimide (NHS), the carboxyl on the graphene oxide (GO) surface was successfully activated into NHS active ester. In this study, bovine serum albumin (BSA) was selected as a model protein, used for studying the protein absorption capacity of the NHS activated GO (GO-EDC-NHS). Approximately 12.75mg of BSA could be covalent bonded onto the GO-EDC-NHS surface (BSA-CB-GO), whereas only 6.83mg of BSA physical absorbed onto the GO surface (BSA-NB-GO). With a 168h of phosphate buffer saline (PBS) soaking, the BSA accumulative desorption ratio, which was accordingly assigned to the BSA-NB-GO and the BSA-CB-GO, was separately 29.91wt% and 2.95wt%. Consequently, it proved GO-EDC-NHS exhibited more stable and stronger BSA absorption capacity. As compared to the mouse bone marrow mesenchymal stem cells (mBMSCs) cultivated on the BSA-NB-GO surface, the immunofluorescence staining images showed that more vinculins and integrin α5 were visible in the mBMSCs cultivated on the BSA-CB-GO surface, they also produced more distinct stress fibers and actin-containing microfilaments. In summary, BSA-CB-GO possesses an excellent cell affinity, which can be considered as a promising functional material used for promoting the bone remodeling. Copyright © 2017 Elsevier B.V. All rights reserved.

Multi-spectroscopic and voltammetric evidences for binding, conformational changes of bovine serum albumin with thiamine.

Science.gov (United States)

Bagoji, Atmanand M; Gowda, Jayant I; Gokavi, Naveen M; Nandibewoor, Sharanappa T

2017-08-01

The interaction between thiamine hydrochloride (TA) and bovine serum albumin (BSA) was investigated by fluorescence, FTIR, UV-vis spectroscopic and cyclic voltammetric techniques under optimised physiological condition. The fluorescence intensity of BSA is gradually decreased upon addition of TA due to the formation of a BSA-TA complex. The binding parameters were evaluated and their behaviour at different temperatures was analysed. The quenching constants (K sv ) obtained were 2.6 × 10 4 , 2.2 × 10 4 and 2.0 × 10 4  L mol -1 at 288, 298 and 308 K, respectively. The binding mechanism was static-type quenching. The values of ΔH° and ΔS° were found to be 26.87 kJ mol -1 and 21.3 J K -1  mol -1 , and indicated that electrostatic interaction was the principal intermolecular force. The changes in the secondary structure of BSA upon interaction with TA were confirmed by synchronous and 3-D spectral results. Site probe studies reveal that TA is located in site I of BSA. The effects of some common metal ions on binding of BSA-TA complex were also investigated.

Characterization of in vitro glucuronidation clearance of a range of drugs in human kidney microsomes: comparison with liver and intestinal glucuronidation and impact of albumin.

Science.gov (United States)

Gill, Katherine L; Houston, J Brian; Galetin, Aleksandra

2012-04-01

Previous studies have shown the importance of the addition of albumin for characterization of hepatic glucuronidation in vitro; however, no reports exist on the effects of albumin on renal or intestinal microsomal glucuronidation assays. This study characterized glucuronidation clearance (CL(int, UGT)) in human kidney, liver, and intestinal microsomes in the presence and absence of bovine serum albumin (BSA) for seven drugs with differential UDP-glucuronosyltransferase (UGT) 1A9 and UGT2B7 specificity, namely, diclofenac, ezetimibe, gemfibrozil, mycophenolic acid, naloxone, propofol, and telmisartan. The impact of renal CL(int, UGT) on accuracy of in vitro-in vivo extrapolation (IVIVE) of glucuronidation clearance was investigated. Inclusion of 1% BSA for acidic drugs and 2% for bases/neutral drugs in incubations was found to be suitable for characterization of CL(int, UGT) in different tissues. Although BSA increased CL(int, UGT) in all tissues, the extent was tissue- and drug-dependent. Scaled CL(int, UGT) in the presence of BSA ranged from 2.22 to 207, 0.439 to 24.4, and 0.292 to 23.8 ml · min(-1) · g tissue(-1) in liver, kidney, and intestinal microsomes. Renal CL(int, UGT) (per gram of tissue) was up to 2-fold higher in comparison with that for liver for UGT1A9 substrates; in contrast, CL(int, UGT) for UGT2B7 substrates represented approximately one-third of hepatic estimates. Scaled renal CL(int, UGT) (in the presence of BSA) was up to 30-fold higher than intestinal glucuronidation for the drugs investigated. Use of in vitro data obtained in the presence of BSA and inclusion of renal clearance improved the IVIVE of glucuronidation clearance, with 50% of drugs predicted within 2-fold of observed values. Characterization and consideration of kidney CL(int, UGT) is particularly important for UGT1A9 substrates.

Synthesis, characterization and serum albumin binding studies of vitamin K3 derivatives.

Science.gov (United States)

Suganthi, Murugesan; Elango, Kuppanagounder P

2017-01-01

Synthesis, characterization and bovine serum albumin (BSA) binding properties of three derivatives of vitamin K3 have been described. Results of UV-Vis and fluorescence spectra indicate complexation between BSA and the ligands with conformational changes in protein, which is strongly supported by synchronous and three dimensional fluorescence studies. Addition of the ligands quenches the fluorescence of BSA which is accompanied by reduction in quantum yield (Ф) from 0.1010 to 0.0775-0.0986 range. Thermodynamic investigations reveal that hydrophobic interaction is the major binding force in the spontaneous binding of these ligands with BSA. The binding constants obtained depend on the substituent present in the quinone ring, which correlates linearly with the Taft's field substituent constant (σ F ). The results show that compound with strong electron withdrawing nitro-group forms relatively stronger complex with BSA than amino and thioglycolate substituted ones. Circular dichroism studies show that the α-helical content of the protein, upon complexation with the ligands, decreases in the case of amino and nitro substituted vitamin K3 while increases in thioglycolate substituted compound. Molecular docking studies indicated that the vitamin K3 derivatives are surrounded by hydrophobic residues of the BSA molecule, which is in good agreement with the results of fluorescence spectral and thermodynamic studies. Copyright © 2016 Elsevier B.V. All rights reserved.

Serum albumin and the haloperidol pharmacokinectics. A study using a computational model

Science.gov (United States)

de Morais e Coura, Carla Patrícia; Paulino, Erica Tex; Cortez, Celia Martins; da Silva Fragoso, Viviane Muniz

2016-12-01

Here we are studying the binding of haloperidol with human and bovine sera albumins applying a computational model, based on spectrofluorimetry, statistical and mathematical knowledge. Haloperidol is one of the oldest antipsychotic drug in use for therapy of patients with acute and chronic schizophrenia. It was found that the fluorescence of HSA was quenched in 18.0 (± 0.2)% and for BSA it was 24.0 (± 0.9)%, for a ratio of 1/1000 of haloperidol/albumin. Results suggested that the primary binding site is located in the subdomain IB. Quenching constants of the albumin fluorescence by haloperidol were in the order of 107, approximately 100-fold higher than that found for risperidone, and about 1000-fold higher than that estimated for chlorpromazine and sulpiride.

Protein-silver nanoparticle interactions to colloidal stability in acidic environments.

Science.gov (United States)

Tai, Jui-Ting; Lai, Chao-Shun; Ho, Hsin-Chia; Yeh, Yu-Shan; Wang, Hsiao-Fang; Ho, Rong-Ming; Tsai, De-Hao

2014-11-04

We report a kinetic study of Ag nanoparticles (AgNPs) under acidic environments (i.e., pH 2.3 to pH ≈7) and systematically investigate the impact of protein interactions [i.e., bovine serum albumin (BSA) as representative] to the colloidal stability of AgNPs. Electrospray-differential mobility analysis (ES-DMA) was used to characterize the particle size distributions and the number concentrations of AgNPs. Transmission electron microscopy was employed orthogonally to provide visualization of AgNPs. For unconjugated AgNPs, the extent of aggregation, or the average particle size, was shown to be increased significantly with an increase of acidity, where a partial coalescence was found between the primary particles of unconjugated AgNP clusters. Aggregation rate constant, kD, was also shown to be proportional to acidity, following a correlation of log(kD) = -1.627(pH)-9.3715. Using ES-DMA, we observe BSA had a strong binding affinity (equilibrium binding constant, ≈ 1.1 × 10(6) L/mol) to the surface of AgNPs, with an estimated maximum molecular surface density of ≈0.012 nm(-2). BSA-functionalized AgNPs exhibited highly-improved colloidal stability compared to the unconjugated AgNPs under acidic environments, where both the acid-induced interfacial dissolution and the particle aggregation became negligible. Results confirm a complex mechanism of colloidal stability of AgNPs: the aggregation process was shown to be dominant, and the formation of BSA corona on AgNPs suppressed both particle aggregation and interfacial dissolution of AgNP samples under acidic environments.

Cu(II) Complexes of Isoniazid Schiff Bases: DNA/BSA Binding and Cytotoxicity Studies on A549 Cell Line

OpenAIRE

Ramadevi, Pulipaka; Singh, Rinky; Prajapati, Akhilesh; Gupta, Sarita; Chakraborty, Debjani

2014-01-01

A series of isonicotinoyl hydrazones have been synthesized via template method and were complexed to Cu(II). The ligands are coordinated to Cu(II) ion through the enolic oxygen and azomethine nitrogen resulting in a square planar geometry. The CT-DNA and bovine serum albumin binding propensities of the compounds were determined spectrophotometrically, the results of which indicate good binding propensity of complexes to DNA and BSA with high binding constant values. Furthermore, the compounds...

Interaction of aconitine with bovine serum albumin and effect of atropine sulphate and glycyrrhizic acid on the binding

International Nuclear Information System (INIS)

Huang Yun; Cui Lijian; Wang Jianming; Huo Kun; Chen Chen; Zhan Wenhong; Wang Yongli

2012-01-01

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 K A and n of aconitine–BSA. ► Support for aconitine detoxification by atropine and glycyrrhizic acid.

Combined spectroscopic and molecular docking techniques to study interaction of Zn (II) DiAmsar with serum albumins

Energy Technology Data Exchange (ETDEWEB)

Bardajee, Ghasem Rezanejade, E-mail: rezanejad@pnu.ac.ir; Hooshyar, Zari; Shafagh, Pegah; Ghiasvand, Samira; Kakavand, Nahaleh

2014-12-15

Zinc (II) diamine-sarcophagine (Zn (II) DiAmsar) as a water soluble hexadentate ligand was synthesized and characterized by nuclear magnetic resonance (NMR), Fourier transform infrared (FT-IR) and UV–visible (UV–vis) spectroscopy. The bindings of Zn (II) DiAmsar with human serum albumin (HSA) and bovine serum albumin (BSA) were investigated under the simulative physiological conditions. To study this binding, the fluorescence spectra in combination with FT-IR, UV–vis, cyclic voltammetry (CV), and molecular docking techniques were used in the present work. The results indicate that Zn (II) DiAmsar quenched effectively the intrinsic fluorescence of HSA and BSA via a static quenching process. The fluorescence quenching data was also used to determine binding sites and binding constants at different temperatures. The calculated thermodynamic parameters (∆G°, ∆H°, and ∆S°) suggest that the binding process occurs spontaneously by involving hydrogen bond and van der Waals interactions. The distance between HSA (or BSA) as a donor and Zn (II) DiAmsar as an acceptor was obtained according to fluorescence resonance energy transfer (FRET). In addition, the docking results revealed the possible binding sites and assess the microenvironment around the bounded Zn (II) DiAmsar.

Spectrophotometric study of the interaction between chlorotetracycline and bovine serum albumin using Eosin Y as site marker with the aid of chemometrics

Science.gov (United States)

Ni, Yongnian; Liu, Qiuhong; Kokot, Serge

2011-01-01

Interaction of chlorotetracycline (CTC) with bovine serum albumin (BSA) was investigated under simulated physiological conditions by spectroscopy with the aid of multivariate curve resolution-alternating least squares (MCR-ALS). Eosin Y was selected as an alternative site I marker on the BSA to study the above molecular interaction. The binding of Eosin Y and CTC to BSA showed that CTC was displaced from CTC-BSA complex by Eosin Y, and Eosin Y-BSA complex was formed. However, the recorded fluorescence spectra of Eosin Y and Eosin Y-BSA overlapped and MCR-ALS was applied to resolve the two-way fluorescence spectra. From the resolved equilibrium concentration profiles, it was observed that Eosin Y competed with CTC in the binding process with BSA; it was also shown that the binding site of CTC on BSA was site I, and this was further confirmed by the fluorescence polarization method. Compared with some common site I markers for BSA, the fluorescence and UV-vis spectral shapes of the Eosin Y-BSA complex were quite different from that of Eosin Y, and this feature facilitated the investigation of the small molecule-BSA interaction.

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)

Baimark, Y.; Srisa-Ard, M.; Srihaman, P.

2012-01-01

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)

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.; Zhang, Dingyuan; Alsaiari, Shahad K.; Lu, Jie; Deng, Lin; Tamanoi, Fuyuhiko; Zink, Jeffrey I.; Khashab, Niveen M.

2016-01-01

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.

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.

Characterization of Bovine Serum Albumin Blocking Efficiency on Epoxy-Functionalized Substrates for Microarray Applications.

Science.gov (United States)

Sun, Yung-Shin; Zhu, Xiangdong

2016-10-01

Microarrays provide a platform for high-throughput characterization of biomolecular interactions. To increase the sensitivity and specificity of microarrays, surface blocking is required to minimize the nonspecific interactions between analytes and unprinted yet functionalized surfaces. To block amine- or epoxy-functionalized substrates, bovine serum albumin (BSA) is one of the most commonly used blocking reagents because it is cheap and easy to use. Based on standard protocols from microarray manufactories, a BSA concentration of 1% (10 mg/mL or 200 μM) and reaction time of at least 30 min are required to efficiently block epoxy-coated slides. In this paper, we used both fluorescent and label-free methods to characterize the BSA blocking efficiency on epoxy-functionalized substrates. The blocking efficiency of BSA was characterized using a fluorescent scanner and a label-free oblique-incidence reflectivity difference (OI-RD) microscope. We found that (1) a BSA concentration of 0.05% (0.5 mg/mL or 10 μM) could give a blocking efficiency of 98%, and (2) the BSA blocking step took only about 5 min to be complete. Also, from real-time and in situ measurements, we were able to calculate the conformational properties (thickness, mass density, and number density) of BSA molecules deposited on the epoxy surface. © 2015 Society for Laboratory Automation and Screening.

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)

Mangaiyarkarasi, Rajendiran; Chinnathambi, Shanmugavel; Aruna, Prakasarao; Ganesan, Singaravelu

2015-01-01

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 3 :Tb 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 3 :Tb 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.

Impact of the alkyl chain length on binding of imidazolium-based ionic liquids to bovine serum albumin

Science.gov (United States)

Zhang, Mengyue; Wang, Ying; Zhang, Hongmei; Cao, Jian; Fei, Zhenghao; Wang, Yanqing

2018-05-01

The effects of six imidazolium-based ionic liquids (ILs) with different alkyl chain length ([CnMim]Cl, n = 2, 4, 6, 8, 10, 12) on the structure and functions of bovine serum albumin (BSA) were studied by multi-spectral methods and molecular docking. ILs with the longer alkyl chain length have the stronger binding interaction with BSA and the greater conformational damage to protein. The effects of ILs on the functional properties of BSA were further studied by the determination of non-enzyme esterase activity, β-fibrosis and other properties of BSA. The thermal stability of BSA was reduced, the rate of the formation of beta sheet structures of BSA was lowered, and the esterase-like activity of BSA were decreased with the increase of ILs concentration. Simultaneous molecular modeling technique revealed the favorable binding sites of ILs on protein. The hydrophobic force and polar interactions were the mainly binding forces of them. The calculated results are in a good agreement with the spectroscopic experiments. These studies on the impact of the alkyl chain length on binding of imidazolium-based ionic liquids to BSA are of great significance for understanding and developing the application of ionic liquid in life and physiological system.

Combined spectroscopies and molecular docking approach to characterizing the binding interaction of enalapril with bovine serum albumin.

Science.gov (United States)

Pan, Dong-Qi; Jiang, Min; Liu, Ting-Ting; Wang, Qi; Shi, Jie-Hua

2017-06-01

The binding interaction between bovine serum albumin (BSA) and enalapril (ENPL) at the imitated physiological conditions (pH = 7.4) was investigated using UV-vis absorption spectroscopy (UV-vis), fluorescence emission spectroscopy (FES), synchronous fluorescence spectroscopy (SFS), Fourier transform infrared spectroscopy (FT-IR), circular dichroism (CD) and molecular docking methods. It can be deduced from the experimental results from the steady-state fluorescence spectroscopic titration that the intrinsic BSA fluorescence quenching mechanism induced by ENPL is static quenching, based on the decrease in the BSA quenching constants in the presence of ENPL with increase in temperature and BSA quenching rates >10 10  L mol -1  sec -1 . This result indicates that the ENPL-BSA complex is formed through an intermolecular interaction of ENPL with BSA. The main bonding forces for interaction of BSA and ENPL are van der Waal's forces and hydrogen bonding interaction based on negative values of Gibbs free energy change (ΔG 0 ), enthalpic change (ΔH 0 ) and entropic change (ΔS 0 ). The binding of ENPL with BSA is an enthalpy-driven process due to |ΔH°| > |TΔS°| in the binding process. The results of competitive binding experiments and molecular docking confirm that ENPL binds in BSA sub-domain IIA (site I) and results in a slight change in BSA conformation, but BSA still retains its α-helical secondary structure. Copyright © 2016 John Wiley & Sons, Ltd.

Polysaccharides-based polyelectrolyte nanoparticles as protein drugs delivery system

Energy Technology Data Exchange (ETDEWEB)

Shu Shujun; Sun Lei; Zhang Xinge, E-mail: zhangxinge@nankai.edu.cn [Nankai University, Key Laboratory of Functional Polymer Materials Ministry of Education, Institute of Polymer Chemistry (China); Wu Zhongming [Tianjin Medical University, Metabolic Diseases Hospital (China); Wang Zhen; Li Chaoxing, E-mail: lcx@nankai.edu.cn [Nankai University, Key Laboratory of Functional Polymer Materials Ministry of Education, Institute of Polymer Chemistry (China)

2011-09-15

Polysaccharides-based nanoparticles were prepared by synthesized quaternized chitosan and dextran sulfate through simple ionic-gelation self-assembled method. Introduction of quaternized groups was intended to increase water solubility of chitosan and make the nanoparticles have broader pH sensitive range which can remain more stable in physiological pH and decrease the loss of protein drugs caused by the gastric cavity. The load of BSA was affected by molecular parameter, i.e., degree of substitution, and average molecular weight of quaternized chitosan, as well as concentration of BSA. Fast release occurred in phosphate buffer solution (pH 7.4) while the release was slow in hydrochloric acid (pH 1.4). The drug release mechanism is Fickian diffusion through release kinetics analysis. Cell uptake demonstrated nanoparicles can internalize into Caco-2 cells, which suggested that nanoparticles had good biocompatibility. No significant conformation change was noted for the released BSA in comparison with native BSA using circular dichroism spectroscopy. This kind of novel composite nanoparticles may be a promising delivery system for oral protein and peptide drugs.

Three-dimensionally porous graphene: A high-performance adsorbent for removal of albumin-bonded bilirubin.

Science.gov (United States)

Ma, Chun Fang; Gao, Qiang; Xia, Kai Sheng; Huang, Zhi Yuan; Han, Bo; Zhou, Cheng Gang

2017-01-01

The development of bilirubin adsorbents with high adsorption efficiencies towards albumin-bonded bilirubin is still a considerable challenge. In this work, a three-dimensionally porous graphene (3D-pGR) has been fabricated through a simple carbon dioxide (CO 2 ) activation of thermally exfoliated graphite oxide (EGO). Intriguingly, the resultant 3D-pGR material showed hierarchically micro-meso-macroporous structure, high specific surface area of up to 843m 2 g -1 , and large pore volume as high as 2.71cm 3 g -1 . Besides, the large planar π-configuration structure of 3D-pGR made it possible to compete effectively with albumin for bilirubin binding. Taking advantages of these fantastic characteristics, the 3D-pGR was demonstrated to be extraordinarily efficient for bilirubin removal from a bovine serum albumin (BSA)-rich solution. Under optimized conditions, the maximum adsorption capacity of 3D-pGR for BSA-bonded bilirubin was up to 126.1mgg -1 , which is not only significantly higher than the adsorption capacities of currently available adsorbents towards albumin-bonded bilirubin, but also superior to those of many reported adsorbents towards free bilirubin. In addition, the hemolysis assay of 3D-pGR indicated that this material had negligible hemolysis effect. Findings from this study may open up important new possibilities for removal of protein-bonded toxins. Copyright © 2016 Elsevier B.V. All rights reserved.

Biophysical study on the interaction of ceftriaxone sodium with bovine serum albumin using spectroscopic methods.

Science.gov (United States)

Pan, Jiongwei; Ye, Zaiting; Cai, Xiaoping; Wang, Liangxing; Cao, Zhuo

2012-12-01

The interaction of ceftriaxone sodium (CS), a cephalosporin antibiotic, with the major transport protein, bovine serum albumin (BSA), was investigated using different spectroscopic techniques such as fluorescence, circular dichroism (CD), and UV-vis spectroscopy. Values of binding parameters for BSA-CS interaction in terms of binding constant and number of binding sides were found to be 9.00 × 10(3), 3.24 × 10(3), and 2.30 × 10(3) M(-1) at 281, 301, and 321 K, respectively. Thermodynamic analysis of the binding data obtained at different temperatures showed that the binding process was spontaneous and was primarily mediated by van der Waals force or hydrogen bonding. CS binding to BSA caused secondary structural alterations in the protein as revealed by CD results. The distance between CS and Trp of BSA was determined as 3.23 nm according to the Förster resonance energy transfer theory. © 2012 Wiley Periodicals, Inc.

Microplasma jet treatment of bovine serum albumin coatings for controlling enzyme and cell attachmenttype="fn" rid="FN1">

Science.gov (United States)

Szili, Endre J.; Becker, Stefanie; Short, Robert D.; Al-Bataineh, Sameer A.

2017-08-01

We investigated a new approach to control protein and cell attachment inside 96-well polystyrene plates. The wells were first coated with bovine serum albumin (BSA) to inhibit cell and protein attachment. The BSA-coated wells were then treated with a helium microplasma jet for increasing times that resulted in gradual removal of BSA from the surface. It was found that the amount of enzyme and cell attachment could be controlled in the wells where BSA was only partially removed by the microplasma jet. In addition to the surface coverage of BSA, the new surface chemistry induced by the microplasma jet treatment also had an important role in the control of enzyme and cell attachment. In summary, microplasma jet treatment of BSA-coated polystyrene wells is a simple and effective method for controlling enzyme and cell attachment. This might find use for high-throughput screening of new cell culture platforms where control over the level protein, enzyme or cell adherence is needed in order to maintain a specific cell function.

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.

Improved anticancer effects of albumin-bound paclitaxel nanoparticle via augmentation of EPR effect and albumin-protein interactions using S-nitrosated human serum albumin dimer.

Science.gov (United States)

Kinoshita, Ryo; Ishima, Yu; Chuang, Victor T G; Nakamura, Hideaki; Fang, Jun; Watanabe, Hiroshi; Shimizu, Taro; Okuhira, Keiichiro; Ishida, Tatsuhiro; Maeda, Hiroshi; Otagiri, Masaki; Maruyama, Toru

2017-09-01

In the latest trend of anticancer chemotherapy research, there were many macromolecular anticancer drugs developed based on enhanced permeability and retention (EPR) effect, such as albumin bound paclitaxel nanoparticle (nab- PTX, also called Abraxane ® ). However, cancers with low vascular permeability posed a challenge for these EPR based therapeutic systems. Augmenting the intrinsic EPR effect with an intrinsic vascular modulator such as nitric oxide (NO) could be a promising strategy. S-nitrosated human serum albumin dimer (SNO-HSA Dimer) shown promising activity previously was evaluated for the synergistic effect when used as a pretreatment agent in nab-PTX therapy against various tumor models. In the high vascular permeability C26 murine colon cancer subcutaneous inoculation model, SNO-HSA Dimer enhanced tumor selectivity of nab-PTX, and attenuated myelosuppression. SNO-HSA Dimer also augmented the tumor growth inhibition of nab-PTX in low vascular permeability B16 murine melanoma subcutaneous inoculation model. Furthermore, nab-PTX therapy combined with SNO-HSA Dimer showed higher antitumor activity and improved survival rate of SUIT2 human pancreatic cancer orthotopic model. In conclusion, SNO-HSA Dimer could enhance the therapeutic effect of nab-PTX even in low vascular permeability or intractable pancreatic cancers. The possible underlying mechanisms of action of SNO-HSA Dimer were discussed. Copyright © 2017 Elsevier Ltd. All rights reserved.

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.

Elucidation of intermolecular interaction of bovine serum albumin with Fenhexamid: A biophysical prospect.

Science.gov (United States)

Shi, Jie-Hua; Lou, Yan-Yue; Zhou, Kai-Li; Pan, Dong-Qi

2018-03-01

Fenhexamid, as a hydroxyanilide, is widely applied to control Botrytis cinerea for protecting crops and fruits. But it could adversely affect human and animals health due to accumulation of residues in food production. Here, the affinity characteristics of fenhexamid on bovine serum albumin (BSA) was studied via a series of spectroscopic methods such as steady-state fluorescence spectroscopy, ultraviolet spectroscopy (UV), synchronous fluorescence spectroscopy (SFS), 3D fluorescence spectroscopy, and fourier transform infrared spectroscopy (FT-IR). The experimental results illustrated that the fluorescence quenching mechanism of BSA induced by fenhexamid was a static quenching. The binding constant (K b ) of fenhexamid with BSA was 2.399 × 10 4  M -1 at 298 K and the combination ratio was about 1:1. The competitive experiment demonstrated that fenhexamid was binding on the BSA at site II (subdomain IIIA), which was confirmed by the molecular docking studies. The negative values of thermodynamic parameter (ΔH 0 , ΔS 0 and ΔG 0 ) revealed that the reaction of fenhexamid with BSA could proceed spontaneously, the van der Waals force and hydrogen bonding interaction conducted the main effect, and the binding process was enthalpy-driven. What's more, the 8-Anilino-1-naphthalenesulfonate (ANS) and sucrose binding studies were also performed and further verified the binding force between BSA and fenhexamid. Copyright © 2018 Elsevier B.V. All rights reserved.

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.

Albumin fibrillization induces apoptosis via integrin/FAK/Akt pathway

Directory of Open Access Journals (Sweden)

Liang Chi-Ming

2009-01-01

Full Text Available Abstract Background Numerous proteins can be converted to amyloid-like fibrils to increase cytotoxicity and induce apoptosis, but the methods generally require a high concentration of protein, vigorous shaking, or fibril seed. As well, the detailed mechanism of the cytotoxic effects is not well characterized. In this study, we have developed a novel process to convert native proteins into the fibrillar form. We used globular bovine serum albumin (BSA as a model protein to verify the properties of the fibrillar protein, investigated its cellular effects and studied the signaling cascade induced by the fibrillar protein. Results We induced BSA, a non-cytotoxic globular protein, to become fibril by a novel process involving Superdex-200 column chromatography in the presence of anionic or zwittergenic detergent(s. The column pore size was more important than column matrix composite in fibril formation. The fibrillar BSA induced apoptosis in BHK-21 cell as well as breast cancer cell line T47D. Pre-treating cells with anti-integrin antibodies blocked the apoptotic effect. Fibrillar BSA, but not globular BSA, bound to integrin, dephosphorylated focal adhesion kinase (FAK, Akt and glycogen synthase kinase-3β (GSK-3β. Conclusion We report on a novel process for converting globular proteins into fibrillar form to cause apoptosis by modulating the integrin/FAK/Akt/GSK-3β/caspase-3 signaling pathway. Our findings may be useful for understanding the pathogenesis of amyloid-like fibrils and applicable for the development of better therapeutic agents that target the underlying mechanism(s of the etiologic agents.

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.

ICAM-1 targeted catalase encapsulated PLGA-b-PEG nanoparticles against vascular oxidative stress.

Science.gov (United States)

Sari, Ece; Tunc-Sarisozen, Yeliz; Mutlu, Hulya; Shahbazi, Reza; Ucar, Gulberk; Ulubayram, Kezban

2015-01-01

Targeted delivery of therapeutics is the favourable idea, whereas it is possible to distribute the therapeutically active drug molecule only to the site of action. For this purpose, in this study, catalase encapsulated poly(D,L-lactide-co-glycolide)-block-poly(ethylene glycol) (PLGA-b-PEG) nanoparticles were developed and an endothelial target molecule (anti-ICAM-1) was conjugated to this carrier system in order to decrease the oxidative stress level in the target site. According to the enzymatic activity results, initial catalase activity of nanoparticles was increased from 27.39 U/mg to up to 45.66 U/mg by adding 5 mg/mL bovine serum albumin (BSA). After 4 h, initial catalase activity was preserved up to 46.98% while free catalase retained less than 4% of its activity in proteolytic environment. Furthermore, FITC labelled anti-ICAM-1 targeted catalase encapsulated nanoparticles (anti-ICAM-1/CatNPs) were rapidly taken up by cultured endothelial cells and concomitantly endothelial cells were resistant to H2O2 induced oxidative impairment.

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.

In-vitro displacement interaction of atenolol and amlodipine on binding with bovine serum albumin when co-administered

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Md. Ashraful Alam, Md. Abdul Awal, Mahbub Mostofa, Md. Kamrul Islam and Nusrat Subhan

2007-06-01

Full Text Available The binding of atenolol (selective β1-blocker and amlodipine (calcium channel blocker to bovine serum albumin (BSA was studied by equilibrium dialysis method in order to have an insight into the binding chemistry of these two to BSA. Free atenolol concentration was increased due to addition of amlodipine which reduced the binding of the compounds to BSA. However, the free fraction was increased to a level as it was expected from direct competitive displacement while the free atenolol concentration was increased according to increasing the amlodipine concentration when only the BSA was present. The result obtained when the binding site was blocked by sufficient amount of amlodipine was that the increment of free concentration of atenolol was prominent. When no amlodipine was added the free concentration of atenolol was only 28% whereas this release was 93 % to 98.01% when amlodipine was added with increasing concentration.

An Improved Method for Removal of Azo Dye Orange II from Textile Effluent Using Albumin as Sorbent

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Tadashi Ohashi

2012-11-01

Full Text Available Azo dyes are generally resistant to biodegradation due to their complex structures. Acid orange II is one of the most widely used dyes in the textile industry. The influence of bovine serum albumin (BSA in different concentrations, pH, and time of contact on Orange II was investigated using kinetics and adsorption-isotherm experiments. The results showed that the maximum colour removed from dye/albumin was 99.50% and that a stable dye-protein complex had been formed at pH 3.5 and in a proportion of 1:3 (v/v, respectively. The synthetic effluent did not show toxicity to the microcrustacean Artemia salina, and showed a CL50 equal to 97 µg/mL to azo dye orange II. Additionally, the methodology was effective in removing the maximum of orange II using BSA by adsorption at pH 3.5 which mainly attracted ions to the azo dye during the adsorption process. This suggests that this form of treatment is economical and easy to use which potentially could lead to bovine serum albumin being used as a sorbent for azo dyes.

Photophysical studies of PET based acridinedione dyes with globular protein: Bovine serum albumin

International Nuclear Information System (INIS)

Rajendran, Kumaran; Perumal, Ramamurthy

2010-01-01

Interaction of acridinedione dyes with model transport proteins, bovine serum albumin (BSA) in aqueous solution were investigated by fluorescence spectral studies. A fluorescence enhancement was observed on the addition of BSA to photoinduced electron transfer (PET) based acridinedione dyes, which posses C 6 H 4 (p-OCH 3 ) in the 9th position of the basic acridinedione ring. On the contrary, the addition of BSA to non-PET based acridinedione dyes with methyl or phenyl substitution in the 9th position does not result in any fluorescence enhancement. The enhancement in the fluorescence intensity is attributed to the suppression of PET process through space between -OCH 3 group and the acridinedione moiety is elucidated by steady state fluorescence measurements. The fluorescence anisotropy value (r) of 0.40 reveals that the motion of the dye molecule is highly constrained and is largely confined to the rigid microenvironment of the protein molecule. The binding constant (K) was found to be in the order of 6.0x10 3 [M] -1 , which implies the existence of hydrophobic interaction between the PET based dye and BSA. Time resolved fluorescence lifetime measurements reveal that the PET based acridinedione dye preferably binds in the hydrophobic interior of BSA.

Effect of bovine serum albumin on the functionality and structure of catanionic surfactant at air–buffer interface

International Nuclear Information System (INIS)

Maiti, Kajari; Bhattacharya, Subhash C.; Moulik, Satya P.; Panda, Amiya K.

2013-01-01

Interaction of bovine serum albumin (BSA) with the solvent spread monolayer of a catanionic surfactant, octadecyltrimethylammonium dodecylsulfate, (C 18 TA + 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 C 18 TA + 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 C 18 TA + 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.

Comparative SPR study on the effect of nanomaterials on the biological activity of adsorbed proteins

International Nuclear Information System (INIS)

Mei, Q.; Chen, Y.; Hong, J.; Chen, H.; Ding, X.; Yin, Y.; Koh, K.; Lee, J.

2012-01-01

Bioactivity of proteins is evaluated to test the adverse effects of nanoparticles interjected into biological systems. Surface plasmon resonance (SPR) spectroscopy detects binding affinity that is normally related to biological activity. Utilizing SPR spectroscopy, a concise testing matrix is established by investigating the adsorption level of bovine serum albumin (BSA) and anti-BSA on the surface covered with 11-mercaptoundecanoic acid (MUA); magnetic nanoparticles (MNPs) and single-walled carbon nanotubes (SWCNTs), respectively. The immunoactivity of BSA on MNPs and SWCNT decreased by 18 % and 5 %, respectively, compared to that on the gold film modified with MUA. This indicates that MNPs cause a considerable loss of biological activity of adsorbed protein. This effect can be utilized for practical applications on detailed biophysical research and nanotoxicity studies. (author)

Investigations on the interactions of aurintricarboxylic acid with bovine serum albumin: Steady state/time resolved spectroscopic and docking studies.

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Bardhan, Munmun; Chowdhury, Joydeep; Ganguly, Tapan

2011-01-10

In this paper, the nature of the interactions between bovine serum albumin (BSA) and aurintricarboxylic acid (ATA) has been investigated by measuring steady state and time-resolved fluorescence, circular dichroism (CD), FT-IR and fluorescence anisotropy in protein environment under physiological conditions. From the analysis of the steady state and time-resolved fluorescence quenching of BSA in aqueous solution in presence of ATA it has been inferred that the nature of the quenching originates from the combined effect of static and dynamic modes. From the determination of the thermodynamic parameters obtained from temperature-dependent changes in K(b) (binding constant) it was apparent that the combined effect of hydrophobic association and electrostatic attraction is responsible for the interaction of ATA with BSA. The effect of ATA on the conformation of BSA has been examined by analyzing CD spectrum. Though the observed results demonstrate some conformational changes in BSA in presence of ATA but the secondary structure of BSA, predominantly of α-helix, is found to retain its identity. Molecular docking of ATA with BSA also indicates that ATA docks through hydrophobic interaction. Copyright © 2010 Elsevier B.V. All rights reserved.

Binding of carbendazim to bovine serum albumin: Insights from experimental and molecular modeling studies

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Li, Jinhua; Zhang, Yulei; Hu, Lin; Kong, Yaling; Jin, Changqing; Xi, Zengzhe

2017-07-01

Carbendazim (CBZ) is a widely used benzimidazole fungicide in agriculture to control a wide range of fruit and vegetable pathogens, which may lead to potential health hazards. To evaluate the potential toxicity of CBZ, the binding mechanism of bovine serum albumin (BSA) with CBZ was investigated by the fluorescence quenching technology, UV absorbance spectra, circular dichroism (CD), and molecular modeling. The fluorescence titration and UV absorbance spectra revealed that the fluorescence quenching mechanism of BSA by CBZ was a combined quenching process. In addition, the studies of CD spectra suggested that the binding of CBZ to BSA changed the secondary structure of protein. Furthermore, the thermodynamic functions of enthalpy change (ΔH0) and entropy change (ΔS0) for the reaction were calculated to be 24.87 kJ mol-1 and 162.95 J mol-1 K-1 according to Van't Hoff equation. These data suggested that hydrophobic interaction play a major role in the binding of CBZ to BSA, which was in good agreement with the result of molecular modeling study.

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

Enhancing intracellular taxane delivery: current role and perspectives of nanoparticle albumin-bound paclitaxel in the treatment of advanced breast cancer.

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Guarneri, Valentina; Dieci, Maria Vittoria; Conte, Pierfranco

2012-02-01

Docetaxel and paclitaxel are among the most active agents for the treatment of breast cancer. These first-generation taxanes are extremely hydrophobic; therefore, solvents are needed for its parenteral administration. Albumin nanoparticle technology allows for the transportation of such hydrophobic drugs without the need of potentially toxic solvents. Nab-paclitaxel can be administered without premedication, in a shorter infusion time and without the need for a special infusion set. Moreover, this technology allows the selective delivery of larger amounts of anticancer drug to tumors, by exploiting endogenous albumin pathways. An overview of the albumin nanoparticle technology, from a clinical perspective, is reported in this paper. The preclinical and clinical development of nab-paclitaxel is reviewed, in the context of available therapies for advanced breast cancer, with a focus on safety data. Preclinical and clinical data on the prognostic and predictive role of SPARC (secreted protein, acidic and rich in cysteine) are also reported. Nab-paclitaxel is approved at present for the treatment of metastatic breast cancer, after the failure of first-line standard therapy, when anthracyclines are not indicated. Efficacy and safety data, along with a more convenient administration, confirm the potential for nab-paclitaxel to become a reference taxane in breast cancer treatment.

Quantization of bovine serum albumin by fluorescence enhancement effects and corresponding binding of macrocyclic host-protein assembly.

Science.gov (United States)

Bardhan, Munmun; Misra, Tapas; Ganguly, Tapan

2012-01-05

The present paper reports the investigations on the spectroscopic behavior of the binary complexes of the dye aurintricarboxylic acid (ATA) with protein bovine serum albumin (BSA) and 18-crown 6 (CW) (ATA·BSA, ATA·CW) and the ternary complex ATA·CW·BSA by using UV-vis steady state and time resolved fluorescence spectroscopy. The primary aim of the work is to determine the protein (BSA) quantization by fluorescence enhancement method and investigate the 'enhancer' activity of crown ether (CW) on it to increase the resolution. Steady state and time resolved fluorescence measurements demonstrated how fluorescence intensity of ATA could be used for the determination of the protein BSA in aqueous solution. The binding of dye (probe/fluorescent medicinal molecule) with protein and the denaturing effect in the polar environment of acetonitrile of the dye protein complex act as drug binding as well as drug release activity. Apart from its basic research point of view, the present study also possesses significant importance and applications in the field of medicinal chemistry. Copyright © 2011 Elsevier B.V. All rights reserved.

A novel approach to preparing magnetic protein microspheres with core-shell structure

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Jiang Wei, E-mail: climentjw@126.co [National Special Superfine Powder Engineering Research Center, Nanjing University of Science and Technology, Nanjing 210094 (China); Sun Zhendong; Li Fengsheng [National Special Superfine Powder Engineering Research Center, Nanjing University of Science and Technology, Nanjing 210094 (China); Chen Kai; Liu Tianyu; Liu Jialing [Department of Physics, Nanjing University of Science and Technology, Nanjing 210094 (China); Zhou Tianle [Department of Materials Science and Engineering, Nanjing University of Science and Technology, Nanjing 210094 (China); Guo Rui [Department of Mechanical Engineering, Nanjing University of Science and Technology, Nanjing 210094 (China)

2011-03-15

Magnetic protein microspheres with core-shell structure were prepared through a novel approach based on the sonochemical method and the emulsion solvent evaporation method. The microspheres are composed of the oleic acid and undecylenic acid modified Fe{sub 3}O{sub 4} cores and coated with globular bovine serum albumin (BSA). Under an optimized condition, up to 57.8 wt% of approximately 10 nm superparamagnetic Fe{sub 3}O{sub 4} nanoparticles could be uniformly encapsulated into the BSA microspheres with the diameter of approximately 160 nm and the high saturation magnetization of 38.5 emu/g, besides of the abundant functional groups. The possible formation mechanism of magnetic microspheres was discussed in detail. - Research Highlights: Magnetic protein microspheres with core-shell structure were prepared through a novel approach based on the sonochemical method and the emulsion solvent evaporation method. The microspheres are composed of the oleic acid and undecylenic acid modified Fe{sub 3}O{sub 4} cores and coated with globular bovine serum albumin (BSA). 57.8 wt% of approximately 10 nm superparamagnetic Fe{sub 3}O{sub 4} nanoparticles could be uniformly encapsulated into the BSA microspheres with the diameter of approximately 160 nm and the high saturation magnetization of 38.5 emu/g, besides the abundant functional groups.

A novel approach to preparing magnetic protein microspheres with core-shell structure

International Nuclear Information System (INIS)

Jiang Wei; Sun Zhendong; Li Fengsheng; Chen Kai; Liu Tianyu; Liu Jialing; Zhou Tianle; Guo Rui

2011-01-01

Magnetic protein microspheres with core-shell structure were prepared through a novel approach based on the sonochemical method and the emulsion solvent evaporation method. The microspheres are composed of the oleic acid and undecylenic acid modified Fe 3 O 4 cores and coated with globular bovine serum albumin (BSA). Under an optimized condition, up to 57.8 wt% of approximately 10 nm superparamagnetic Fe 3 O 4 nanoparticles could be uniformly encapsulated into the BSA microspheres with the diameter of approximately 160 nm and the high saturation magnetization of 38.5 emu/g, besides of the abundant functional groups. The possible formation mechanism of magnetic microspheres was discussed in detail. - Research Highlights: → Magnetic protein microspheres with core-shell structure were prepared through a novel approach based on the sonochemical method and the emulsion solvent evaporation method.→ The microspheres are composed of the oleic acid and undecylenic acid modified Fe 3 O 4 cores and coated with globular bovine serum albumin (BSA).→ 57.8 wt% of approximately 10 nm superparamagnetic Fe 3 O 4 nanoparticles could be uniformly encapsulated into the BSA microspheres with the diameter of approximately 160 nm and the high saturation magnetization of 38.5 emu/g, besides the abundant functional groups.

Erlotinib-loaded albumin nanoparticles: A novel injectable form of erlotinib and its in vivo efficacy against pancreatic adenocarcinoma ASPC-1 and PANC-1 cell lines.

Science.gov (United States)

Noorani, M; Azarpira, N; Karimian, K; Heli, H

2017-10-05

Erlotinib was loaded on albumin nanoparticles for the first time and the cytotoxic effect of the resulting nanoparticles against ASPC-1 and PANC-1 pancreatic adenocarcinoma cell lines was evaluated. The carrier (albumin nanoparticles, ANPs) was synthesized by desolvation method using a mixed solvent followed by thermal crosslinking for stabilization. ANPs and the drug-loaded ANPs were characterized by field emission scanning and transmission electron microscopies, particle size analysis and Fourier transform infrared spectroscopy. The nanoformulation had a size of PANC-1 cell line). Values of IC 50 were obtained for both cell lines and indicated significant reduction in the erlotinib dose necessary for killing the cells, while, ANPs were completely safe. The results demonstrated that erlotinib-loaded ANPs had a remarkable potential for pancreatic cancer drug delivery. Copyright © 2017 Elsevier B.V. All rights reserved.

Fluorescence resonance energy transfer: A promising tool for investigation of the interaction between 1-anthracene sulphonate and serum albumins

International Nuclear Information System (INIS)

Banerjee, Paltu; Ghosh, Saptaparni; Sarkar, Arindam; Bhattacharya, Subhash Chandra

2011-01-01

This present investigation has revealed that steady state as well as time-resolved fluorescence techniques can serve as highly sensitive monitors for exploring the interaction of fluorescent probe 1-anthracene sulphonate (1-AS) with model transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA).We have focused on fluorescence resonance energy transfer (FRET) between excited tryptophan in transport proteins to 1-AS, for the study of relaxation dynamics of biological molecules.

Comparative study of the interactions between bisphenol-A and its endocrine disrupting analogues with bovine serum albumin using multi-spectroscopic and molecular docking studies.

Science.gov (United States)

Ikhlas, Shoeb; Usman, Afia; Ahmad, Masood

2018-04-24

Interaction studies of bisphenol analogues; biphenol-A (BPA), bisphenol-B (BPB), and bisphenol-F (BPF) with bovine serum albumin (BSA) were performed using multi-spectroscopic and molecular docking studies at the protein level. The mechanism of binding of bisphenols with BSA was dynamic in nature. SDS refolding experiments demonstrated no stabilization of BSA structure denatured by BPB, however, BSA denatured by BPA and BPF was found to get stabilized. Also, CD spectra and molecular docking studies revealed that BPB bound more strongly and induced more conformational changes in BSA in comparison to BPA. Hence, this study throws light on the replacement of BPA by its analogues and whether the replacement is associated with a possible risk, raising a doubt that perhaps BPB is not a good substitute of BPA.

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. Copyright © 2013 Elsevier B.V. All rights reserved.

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)