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Showing papers on "Bovine serum albumin published in 2006"


Journal ArticleDOI
TL;DR: Aggregation in poor solvents and complexation with calf thymus DNA and bovine serum albumin turn "on" the fluorescence of tetraphenylethylene derivatives, due to the restriction of intra-molecular rotations of the dyes in the aggregates and complexes.

490 citations


Journal ArticleDOI
TL;DR: Experimental results showed that the binding of GEM to BSA or HSA induced conformational changes in BSA and HSA, and confirmed that the secondary structure of protein was altered by GEM.

477 citations


Journal ArticleDOI
TL;DR: The complexes of a carboxylate-substituted poly(para-phenyleneethynylene) (PPE) with histone, bovine serum albumin, and papain were investigated, and the observed selectivities and sensitivities are most unusual.
Abstract: The complexes of a carboxylate-substituted poly(para-phenyleneethynylene) (PPE) with histone, bovine serum albumin, and papain were investigated. At higher concentrations, the proteins have a significant effect on the emission characteristics of the PPE. The electrostatic complexes formed from the PPE, and the proteins are agglutinated by different metal cations. The observed selectivities and sensitivities of these simple systems are most unusual; combination of the carboxylate-PPE and commercially available papain forms an electrostatic complex that is precipitated by mercury ions at concentrations above 10-5 mol L-1.

316 citations


Journal ArticleDOI
Yan-Jun Hu1, Yi Liu1, Ru-Ming Zhao1, Jia-Xin Dong1, Song-Sheng Qu1 
TL;DR: In this paper, the interaction between methylene blue (MB) and bovine serum albumin (BSA) was investigated by fluorescence and UV-vis absorbance spectroscopy.
Abstract: The interaction between methylene blue (MB) and bovine serum albumin (BSA) was investigated by fluorescence and UV–vis absorbance spectroscopy. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by MB is mainly a result of the formation of MB–BSA complex and electrostatic interactions play an important role to stabilize the complex. The Stern–Volmer quenching constant K SV and corresponding thermodynamic parameters Δ H , Δ G , and Δ S were calculated. The distance r between donor (BSA) and acceptor (MB) was obtained according to fluorescence resonance energy transfer (FRET). The effect of MB on the conformation of BSA has been analyzed by means of UV–vis absorbance spectra and synchronous fluorescence spectroscopy.

267 citations


Journal ArticleDOI
TL;DR: Proteins were screened by preparing dispersions of SWNTs to investigate the driving force of the interaction between single-walled carbon nanotubes (SWNTs) of mean diameter 1 nm and water-soluble proteins, and far-UV circular dichroism spectra indicated that the LYS and BSA molecules that coat SWNT surfaces were partially denatured.

214 citations


Journal ArticleDOI
TL;DR: Co-axial electrospinning is shown to be a versatile technique in achieving the delivery of biochemical signals in a controlled manner for regenerative medicine applications.

202 citations


Journal ArticleDOI
TL;DR: Results indicate that renal tubular cells exposed to high protein load suffer from ER stress, and ER stress may subsequently lead to tubular damage by activation of caspase-12.

188 citations


Journal ArticleDOI
TL;DR: Sorbol, at concentrations from 0 to 2 M, led to the progressive restoration of BSA volume and compressibility values, as well as a substantial recovery of its original alpha-helix content, implying that the compressibility variation observed reflects the conformational changes during the transition.

178 citations


Journal ArticleDOI
TL;DR: The two techniques applied in the present study -- micro-DSC and FTIR spectroscopy -- can be concluded to provide complementary information on adsorption-induced structural changes on both the molecular and sub-molecular level (secondary structure).

167 citations


Journal ArticleDOI
TL;DR: K(i) values determined under certain experimental conditions may quantitatively predict inhibition of UGT catalysed drug glucuronidation in vivo.
Abstract: Aims Using the fluconazole–zidovudine (AZT) interaction as a model, to determine whether inhibition of UDP–glucuronosyltransferase (UGT) catalysed drug metabolism in vivo could be predicted quantitatively from in vitro kinetic data generated in the presence and absence bovine serum albumin (BSA).

166 citations


Journal ArticleDOI
TL;DR: Nano-crystalline Zn-containing hydroxyapatite (ZnHAp) was prepared by the wet-chemical method and the selective adsorption of essential proteins was examined, taking bovine serum albumin and pathogenic protein such as beta(2)-microglobulin (beta( 2)-MG) as model proteins.

Journal ArticleDOI
TL;DR: Gly-BSA stimulates cardiomyocyte ROS production through a protein kinase C–dependent activation of a Nox2-containing NADPH oxidase, which results in nuclear factor-&kgr;B activation and upregulation of atrial natriuretic factor mRNA.
Abstract: Background— Nonenzymatic glycation that results in the production of early-glycation Amadori-modified proteins and advanced-glycation end products may be important in the pathogenesis of diabetic complications. However, the effects of early-glycated proteins, such as glycated serum albumin (Gly-BSA), are poorly defined. In this study, we investigated the effects of Gly-BSA on reactive oxygen species (ROS) production by cardiomyocytes. Methods and Results— Cultured neonatal rat cardiomyocytes were incubated with Gly-BSA or vehicle (bovine serum albumin [BSA]) for up to 48 hours. Gly-BSA dose-dependently increased in situ ROS production (whole-cell dichlorodihydrofluorescein fluorescence), with an optimum effect at 400 μg/mL after 24-hour incubation (152±10% versus BSA 100%; P<0.01). Treatment with the NADPH oxidase inhibitor apocynin, a Nox2 (gp91phox) antisense oligonucleotide (Nox2 AS), or the peptide gp91ds-tat significantly reduced Gly-BSA–induced ROS production at 24 hours (68.5±2.2%, 61.4±8.3%, and 5...

Journal ArticleDOI
01 Apr 2006-Langmuir
TL;DR: Polymer synthesis, derivatization, and swelling, as well as BSA immobilization kinetics and thermodynamics were characterized using reflectance FT-IR spectroscopy, ellipsometry, and protein assays.
Abstract: Polymeric coatings with high protein-binding capacities are important for increasing the output of affinity-based protein purification and decreasing the detection limits of antibody microarrays. This report describes the use of thick poly(acrylic acid) (PAA) brushes to immobilize as much as 80 monolayers of protein. The brushes were prepared using a recently developed procedure that allows polymerization of 100-nm-thick poly(tert-butyl acrylate) films from a surface in just 5 min along with hydrolysis of these films to PAA in 15 min. Covalent binding of bovine serum albumin (BSA) to PAA brushes that were activated using standard coupling agents, however, resulted in immobilization of less than two monolayers of BSA because of competitive hydrolysis of the esters in the activated film. In contrast, derivatization of PAA with nitrilotriacetate (NTA)−Cu2+ complexes yielded films capable of binding many monolayers of protein via metal-ion affinity interactions. For example, derivatization of 55-nm-thick PAA ...

Journal ArticleDOI
TL;DR: In this study microwave technology was used to develop a fast protein preparation and enzymatic digestion method for protein mixtures, which enabled preparation and digestion ofprotein mixtures in solution or in gel in 6 or 25 min, respectively.

Journal ArticleDOI
TL;DR: In this paper, the interaction between 3,3-bis(4-hydroxy-1-naphthyl)-phthalide (NPP) and bovine serum albumin (BSA) was studied by fluorescence spectroscopy.
Abstract: The interaction between 3,3-bis(4-hydroxy-1-naphthyl)-phthalide (NPP) and bovine serum albumin (BSA) have been studied by fluorescence spectroscopy. The binding of NPP quenches the BSA fluorescence. By the fluorescence quenching results, it was found that the binding constant K = 5.30 × 10 4 L mol −1 , and number of binding sites n = 0.9267. In addition, according to the synchronous fluorescence spectra of BSA, the results showed that the fluorescence spectra of BSA mainly originate from the tryptophan residues. Finally, the distance between the acceptor NPP and BSA was estimated to be 1.94 nm using Foster's equation on the basis of fluorescence energy transfer. The interaction between NPP and BSA has been verified as consistent with the static quenching procedure and the quenching mechanism is related to the energy transfer.

Journal ArticleDOI
TL;DR: Tiglycine, diglytine and glycine, in decreasing order, were effective in lowering the final level of colored melanin formed by the action of polyphenol oxidase on DL-DOPA.
Abstract: Casein hydrolyzate and bovine serum albumin did not inhibit the o-dihydroxyphenolase activity of polyphenol oxidase of avocado and mushroom. L-lysine, glycine, L-histidine and L-phenylalanine, in increasing order of effectiveness, inhibited o-dihydroxyphenolase activity to a maximum of about 60% inhibition only; 50% inhibition was observed with 50 mM L-phenylalanine vs. 160 mM L-lysine. L-cysteine at about 0.4 mM gave full inhibition. Triglycine, diglytine and glycine, in decreasing order, were effective in lowering the final level of colored melanin formed by the action of polyphenol oxidase on DL-DOPA. Amino acids are nontoxic and could be safely added to food during processins as a means of preventing undesirable enzymatic browning.

Journal ArticleDOI
06 Dec 2006-Scanning
TL;DR: It is found that BSA and LYZ can be readily immobilized on SAMs at their isoelectric point (IEP), and the strong hydrophobic interaction at the IEP is attributed to immobilization.
Abstract: The immobilization of protein molecules on self-assembled monolayers (SAM) by physical interactions and chemical bonding has been studied using atomic force microscopy (AFM). The proteins used for our investigation are bovine serum albumin (BSA), lysozyme (LYZ), and normal rabbit immunoglobulin G (IgG). The surfaces are methyl-, hydroxyl-, carboxylic acid- and aldehyde-terminated SAMs. We found that BSA and LYZ can be readily immobilized on SAMs at their isoelectric point (IEP). The detailed surface morphology of adsorbed proteins varies with the functionality of the SAMs. The strong hydrophobic interaction at the IEP is attributed to immobilization. If the solution pH is deviated from the IEP, proteins may be attached onto the surface via electrostatic interactions. Covalent binding between the aldehyde-terminated SAM and the H2N-groups in the protein results in immobilization of all three proteins. The individual proteins and their orientations on SAMs are clearly resolved from high-resolution AFM images. The stability and bioactivity of these immobilized proteins are also studied.

Journal ArticleDOI
TL;DR: In this paper, the thermal denaturation process of bovine and human both fatty acid containing and fatty acid free albumins in aqueous solution was studied by use of differential scanning calorimetry.
Abstract: The thermal denaturation process of bovine and human both fatty acid containing and fatty acid free albumins in aqueous solution was studied by use of differential scanning calorimetry. Human serum albumins were found to be more stable than their bovine counterparts. Fatty acid free albumins were characterized as generally less stable, more susceptible to aggregation, their unfolding endothermic transition was less cooperative and with the smaller degree of reversibility. Deconvolution analysis with using a non-two-state model with two component transitions showed essential differences in the thermodynamic parameters between all studied albumins, particularly regarding the high-temperature component transition.

Journal ArticleDOI
TL;DR: The results of the research show that the as-prepared Ag2S nanorods are monodispersed with sizes about 40 nm in diameter and 220 nm in length, and exhibit a high degree of crystallinity and good photoluminescence.
Abstract: Highly ordered silver sulfide nanorods conjugated with the Bovine Serum Albumin (BSA) protein have been successfully achieved at ambient temperature. Such a process is very simple and controllable, directly using silver nitrate and thioacetamide (TAA) as the reactants in the aqueous solution of BSA. The products have been characterized by XRD, HRTEM-SAED, SEM-EDS, TG-DTA, FT-IR, and CD spectroscopy. The results of the research show that the as-prepared Ag2S nanorods are monodispersed with sizes about 40 nm in diameter and 220 nm in length, and exhibit a high degree of crystallinity and good photoluminescence. Furthermore, an interesting mechanism is discussed for the formation of the Ag2S nanorods.

Journal ArticleDOI
TL;DR: The use of atom transfer radical polymerization to grow poly(2-hydroxyethyl methacrylate) brushes in porous alumina followed by functionalization of the PHEMA with nitrilotriacetate−Cu2+ complexes yields membranes that adsorb proteins via coordination of Cu2+ to histidine residues that have unusually high capacity for rapid protein binding.
Abstract: The use of atom transfer radical polymerization to grow poly(2-hydroxyethyl methacrylate) (PHEMA) brushes in porous alumina followed by functionalization of the PHEMA with nitrilotriacetate−Cu2+ complexes yields membranes that adsorb proteins via coordination of Cu2+ to histidine residues. Adsorption isotherms show that these membranes have binding capacities as high as 0.9 mg of bovine serum albumin (BSA)/cm2 of external membrane surface area (150 mg/cm3 of membrane), and breakthrough curves indicate that saturation of the membranes with BSA or myoglobin occurs in less than 15 min. The efficiency of protein elution with ethylenediaminetetraacetic acid (EDTA) solutions is essentially 100%, and the membranes show no detectable decrease in capacity over nine cycles of binding, elution, and regeneration with Cu2+. The unusually high capacity of these membranes for rapid protein binding makes them attractive for applications such as purification of His-tag proteins.

Journal ArticleDOI
Hongwei Zhao1, Min Ge1, Zhaoxia Zhang1, Wenfeng Wang1, Guozhong Wu1 
TL;DR: Intrinsic fluorescence emission spectra of serum albumin in the presence of RF show that the endogenous photosensitizer acts as a quencher and the decrease of fluorescence intensity at about 350 nm is attributed to changes in the environment of the protein fluorophores caused by the ligand.

Journal ArticleDOI
Yan-Jun Hu1, Yi Liu1, Ting-Quan Sun, Ai-Min Bai, Jian-Quan Lü, Zhen-Bang Pi1 
TL;DR: It was proved that the fluorescence quenching of BSA by Intal is a result of the formation of Intal-BSA complex and the distance R between the donor and acceptor has been obtained.

Journal ArticleDOI
TL;DR: Coating of substrates with polyelectrolyte multilayers terminated with poly(acrylic acid) (PAA) followed by activation of the free -COOH groups of PAA provides a surface that readily reacts with amine groups to allow covalent immobilization of antibodies.
Abstract: Coating of substrates with polyelectrolyte multilayers terminated with poly(acrylic acid) (PAA) followed by activation of the free −COOH groups of PAA provides a surface that readily reacts with amine groups to allow covalent immobilization of antibodies. The use of this procedure to prepare arrays of antibodies in porous alumina supports facilitates construction of a flow-through system for analysis of fluorescently labeled antigens. Detection limits in the analysis of Cy5-labeled IgG are 0.02 ng/mL because of the high surface area of the alumina membrane, and the minimal diameter of the substrate pores results in binding limited by kinetics, not mass transport. Moreover, PAA-terminated films resist nonspecific protein adsorption, so blocking of antibody arrays with bovine serum albumin is not necessary. These microarrays are capable of effective analysis in 10% fetal bovine serum.

Journal ArticleDOI
15 Sep 2006-Talanta
TL;DR: The synchronous fluorescence spectra show that the microenvironment of the tryptophan residues has not obvious changes, which obeys the phase distribution model and the thermodynamic data show that biliverdin molecules enter the hydrophobic cavity of BSA via hydrophilic interaction.

Journal ArticleDOI
01 Dec 2006
TL;DR: Adsorption and desorption behavior of Bovine Serum Albumin on surface-modified magnetic nanoparticles covered with thermosensitive polymer (PNIPAM) was investigated as a function of temperature, pH, and ionic strength.
Abstract: Adsorption and desorption behavior of Bovine Serum Albumin (BSA) on surface-modified magnetic nanoparticles covered with thermosensitive polymer (PNIPAM) was investigated as a function of temperature, pH, and ionic strength. Functionalization of surface-modified magnetic particles was performed by seed polymerization using N-isopropylacrylamide (PNIPAM) as the main monomer. Characterization of these particles was carried out using transmission electron micrography (TEM), and vibrating sample magnetometry (VSM). The adsorption results exhibited both pH and temperature sensitivity. The results showed that the temperature effect on adsorption/desorption behavior was mainly dependent on the properties of the particles' surface. The effect of pH was also investigated and it was observed that a smaller amount of protein was adsorbed at higher pH because of the electrostatic repulsive force between protein molecules and latex particles. The maximum amount of protein was adsorbed near the isoelectric point of BSA. Desorption results showed that more protein was desorbed when adsorption was done at lower temperatures and desorption efficiency was found to be higher than 80%.

Journal ArticleDOI
TL;DR: Antibody binding to bovine serum albumin and human serumalbumin immobilized onto gold nanoparticles was studied by means of localized surface plasmon resonance (LSPR) spectroscopy and response attributable to the binding of anti-BSA and anti-HSA to BSA- and HSA-functionalized Au nanoparticles, respectively.
Abstract: Antibody binding to bovine serum albumin (BSA) and human serum albumin (HSA) immobilized onto gold nanoparticles was studied by means of localized surface plasmon resonance (LSPR) spectroscopy. Amine-modified glass was prepared by self-assembly of amine-terminated silane on substrate, and gold (Au) nanoparticles were deposited on the amine-modified glass substrate. Au nanoparticles deposited on the glass surface were functionalized by BSA and HSA. BSA immobilization was confirmed by LSPR spectroscopy in conjunction with surface-enhanced Raman scattering spectroscopy. Then, LSPR response attributable to the binding of anti-BSA and anti-HSA to BSA- and HSA-functionalized Au nanoparticles, respectively, was examined. Anti-HSA at levels larger than ∼10 nM could be detected by HSA-immobilized chips with LSPR optical response, which was saturated at concentrations greater than ∼650 nM of anti-HSA.

Journal ArticleDOI
TL;DR: In this article, the binding of isothipendyl hydrochloride (IPH) to bovine serum albumin (BSA) was investigated by fluorescence spectroscopy combined with UV-visible absorption and circular dichroism (CD) techniques under simulative physiological conditions for the first time.

Journal ArticleDOI
TL;DR: It is concluded that the non-covalent epicatechin-BSA complex is formed by hydrogen bonding, indicating an enthalpy driven exothermic interaction.

Journal ArticleDOI
TL;DR: The experiments prove that there is a direct interaction between phenols and DNA or BSA and suggest that used acids can intercalate to DNA and interact strongly with BSA.
Abstract: In the present investigation, an attempt has been made to study the interaction of chosen polyphenols (tannic, ellagic and gallic acids) with calf thymus DNA and bovine serum albumin (BSA) employing spectrofluorimetric technique. The fluorescence quenching of DNA-bound ethidium bromide (EB) and BSA-bound 1-anilinonaphthalene-8-sulfonic acid (ANS) by phenolic acids has been examined. As BSA contains two tryptophan residues, the polyphenols influence on protein by measuring the changes in the fluorescence of BSA in the presence of phenolic acids was also evaluated. Our experiments prove that there is a direct interaction between phenols and DNA or BSA. The obtained data suggest that used acids can intercalate to DNA and interact strongly with BSA. The strongest interactions were observed between DNA and ellagic acid and between BSA and tannic acid. The conformational changes were revealed in DNA and BSA after incubation with tested phenolic acids and the extent depended on the phenol structure and the used concentration.

Journal ArticleDOI
TL;DR: The results provide direct evidence that ascorbate could give rise to a significant false-positive signal in the biotin switch assay, and care should be taken when this method is used.