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Showing papers on "Bovine serum albumin published in 2013"


Journal ArticleDOI
TL;DR: A 1,8-naphthalimide-derived fluorescent probe for H2S based on the thiolysis of dinitrophenyl ether is reported, which exhibits turn-on fluorescence detection of H 2S in bovine serum and lysosome-targetable fluorescent imaging of H1S with excellent selectivity.

278 citations


Journal ArticleDOI
20 Nov 2013-ACS Nano
TL;DR: The disparate effects of a givenprotein corona on particle-cell interactions are demonstrated, highlighting the correlation between protein corona conformation in situ and relevant biological characteristics for biological functionalities.
Abstract: Many biomolecules, mainly proteins, adsorb onto polymer particles to form a dynamic protein corona in biological environments. The protein corona can significantly influence particle-cell interactions, including internalization and pathway activation. In this work, we demonstrate the differential roles of a given protein corona formed in cell culture media in particle uptake by monocytes and macrophages. By exposing disulfide-stabilized poly(methacrylic acid) nanoporous polymer particles (PMASH NPPs) to complete cell growth media containing 10% fetal bovine serum, a protein corona, with the most abundant component being bovine serum albumin, was characterized. Upon adsorption onto the PMASH NPPs, native bovine serum albumin (BSA) was found to undergo conformational changes. The denatured BSA led to a significant decrease in internalization efficiency in human monocytic cells, THP-1, compared with the bare particles, due to reduced cell membrane adhesion. In contrast, the unfolded BSA on the NPPs triggered class A scavenger receptor-mediated phagocytosis in differentiated macrophage-like cells (dTHP-1) without a significant impact on the overall internalization efficiency. Taken together, this work demonstrates the disparate effects of a given protein corona on particle-cell interactions, highlighting the correlation between protein corona conformation in situ and relevant biological characteristics for biological functionalities.

246 citations


Journal ArticleDOI
01 Apr 2013-Carbon
TL;DR: The results demonstrated that, the rGONRs could penetrate into the cells and cause DNA fragmentations as well as chromosomal aberrations, even at low concentration of 1.0 μg/mL after short exposure time of 1 h.

236 citations


Journal ArticleDOI
22 Apr 2013-ACS Nano
TL;DR: This work shows for the first time solid state nanopore measurements of mammalian prion protein, which in its abnormal form is associated with transmissible spongiform encephalopathies, and provides a basis for protein characterization and the study of protein conformational diseases by nanopore detection.
Abstract: Nanopores can be used to detect and analyze single molecules in solution. We have used glass nanopores made by laser-assisted capillary-pulling, as a high-throughput and low cost method, to detect a range of label-free proteins: lysozyme, avidin, IgG, β-lactoglobulin, ovalbumin, bovine serum albumin (BSA), and β-galactosidase in solution. Furthermore, we show for the first time solid state nanopore measurements of mammalian prion protein, which in its abnormal form is associated with transmissible spongiform encephalopathies. Our approach provides a basis for protein characterization and the study of protein conformational diseases by nanopore detection.

232 citations


Journal ArticleDOI
20 Nov 2013-Langmuir
TL;DR: A library of spherical and rod-shaped gold nanoparticles (GNPs) was used to evaluate the process of protein adsorption to their surfaces, and equilibrium binding constant determinations indicated that BSA has a comparable binding affinity to all of the GNPs tested, regardless of surface charge.
Abstract: Investigating the adsorption process of proteins on nanoparticle surfaces is essential to understand how to control the biological interactions of functionalized nanoparticles. In this work, a library of spherical and rod-shaped gold nanoparticles (GNPs) was used to evaluate the process of protein adsorption to their surfaces. The binding of a model protein (bovine serum albumin, BSA) to GNPs as a function of particle shape, size, and surface charge was investigated. Two independent comparative analytical methods were used to evaluate the adsorption process: steady-state fluorescence quenching titration and affinity capillary electrophoresis (ACE). Although under favorable electrostatic conditions kinetic analysis showed a faster adsorption of BSA to the surface of cationic GNPs, equilibrium binding constant determinations indicated that BSA has a comparable binding affinity to all of the GNPs tested, regardless of surface charge. BSA was even found to adsorb strongly to GNPs with a pegylated/neutral surf...

223 citations


Journal ArticleDOI
TL;DR: In this paper, the interaction of various nanomaterials, antibiotics, anticancer drugs, anti-inflammatory agents, dyes, flavonoids, and certain noxious materials with serum albumin is discussed.
Abstract: The interactions of human and bovine serum albumins (HSA and BSA) with various drugs and nanomaterials receive great attention in the recent years owing to their significant impact in the biomedical field. Although there are various techniques available for studying such interactions, fluorescence spectroscopy is the most appealing one due to its high sensitivity and straightforwardness. Detailed information about the interactions of drugs and nanomaterials with serum can be deducted from a mass of information accumulated by the fluorescence quenching studies. The present review emphasizes the interaction of various nanomaterials, antibiotics, anticancer drugs, anti-inflammatory agents, dyes, flavonoids, and certain noxious materials with HSA and BSA. In particular, we focus on the interactions of serum albumin with nanomaterials having different size and stabilizing agents with various receptors. This review helps in understanding the structural features of drugs/nanomaterials crucial for not only their affinity for serum albumin but also their optimum pharmacological activities.

186 citations


Journal ArticleDOI
TL;DR: The formation of the BSA corona presented here provides a low-cost bio-compatible strategy for nanoparticle stabilization and transport in highly ionic environments.
Abstract: We find that citrate-stabilized gold nanoparticles aggregate and precipitate in saline solutions below the NaCl concentration of many bodily fluids and blood plasma. Our experiments indicate that this is due to complexation of the citrate anions with Na+ cations in solution. A dramatically enhanced colloidal stability is achieved when bovine serum albumin is adsorbed to the gold nanoparticle surface, completely preventing nanoparticle aggregation under harsh environmental conditions where the NaCl concentration is well beyond the isotonic point. Furthermore, we explore the mechanism of the formation of this albumin “corona” and find that monolayer protein adsorption is most likely ruled by hydrophobic interactions. As for many nanotechnology-based biomedical and environmental applications, particle aggregation and sedimentation are undesirable and could substantially increase the risk of toxicological side effects; the formation of the BSA corona presented here provides a low-cost biocompatible strategy f...

172 citations


Journal ArticleDOI
TL;DR: A remarkable decrease in the in vitro DL cell proliferation and induction of the apoptosis by 1-4 is revealed, which lies in the order 2 > 1 > 4 > 3.
Abstract: Syntheses and characterizations of the arene ruthenium [(η6-C6H6)RuCl(4-mtdpm)] (1), [(η6-p-MeC6H4Pri)RuCl(4-mtdpm)] (2), and structurally analogous rhodium/iridium complexes [(η5-C5Me5)RhCl(4-mtdpm)] (3) and [(η5-C5Me5)IrCl(4-mtdpm)] (4) [4-mtdpm = 5-(4-methylthiophenyl)dipyrromethene] have been reported. Their identities have been established by satisfactory elemental analyses, electrospray ionization-mass spectrometry (ESI-MS), FT-IR, NMR (1H, 13C), UV/vis, emission spectral, and electrochemical studies. Structure of the representative complex 3 has been authenticated by X-ray single crystal analyses. The complexes 1–4 effectively bind with calf thymus DNA (CT DNA) through intercalative/electrostatic interactions. In addition, these exhibit significant cytotoxicity toward Dalton lymphoma (DL) cell line and cause static quenching of the bovine serum albumin (BSA) fluorophore. The antiproliferative activity, morphological changes, and apoptosis have been evaluated by MTT assay, acridine orange/ethidium b...

140 citations


Journal ArticleDOI
TL;DR: This is the first work to develop an amino acid-based zwitterionic polymer as an antifouling material, demonstrating that pSerMA is a promising alternative to the traditional ethylene glycol-based antifOUling materials.

137 citations


Journal ArticleDOI
15 Feb 2013-ACS Nano
TL;DR: Results with TiO2 nanoparticles in KF demonstrate an association between medium composition, particle uptake, and nanoparticle interaction with cells, leading to chromosomal damage as measured by the MN assay.
Abstract: The widespread use of titanium dioxide (TiO2) nanoparticles in consumer products increases the probability of exposure to humans and the environment. Although TiO2 nanoparticles have been shown to induce DNA damage (comet assay) and chromosome damage (micronucleus assay, MN) in vitro, no study has systematically assessed the influence of medium composition on the physicochemical characteristics and genotoxicity of TiO2 nanoparticles. We assessed TiO2 nanoparticle agglomeration, cellular interaction, induction of genotoxicity, and influence on cell cycle in human lung epithelial cells using three different nanoparticle-treatment media: keratinocyte growth medium (KGM) plus 0.1% bovine serum albumin (KB); a synthetic broncheoalveolar lavage fluid containing PBS, 0.6% bovine serum albumin and 0.001% surfactant (DM); or KGM with 10% fetal bovine serum (KF). The comet assay showed that TiO2 nanoparticles induced similar amounts of DNA damage in all three media, independent of the amount of agglomeration, cellular interaction, or cell-cycle changes measured by flow cytometry. In contrast, TiO2 nanoparticles induced MN only in KF, which is the medium that facilitated the lowest amount of agglomeration, the greatest amount of nanoparticle cellular interaction, and the highest population of cells accumulating in S phase. These results with TiO2 nanoparticles in KF demonstrate an association between medium composition, particle uptake, and nanoparticle interaction with cells, leading to chromosomal damage as measured by the MN assay.

122 citations


Journal ArticleDOI
TL;DR: The proposed aptasensor is successfully used to IgE analysis in human serum sample and the obtained result is well agreed with the value obtained by the standard ELISA method.

Journal ArticleDOI
TL;DR: Surface charge, ionic strength and biological molecules alter the properties of silica NPs and potentially affect their biological effects and there is a need to pre-incubate NPs in the serum to control the composition of the bio-nano-composite that would be present in the human body.
Abstract: Background: Many toxicological studies on silica nanoparticles (NPs) have been reported, however, the literature often shows various conclusions concerning the same material. This is mainly due to a lack of sufficient NPs characterization as synthesized as well as in operando. Many characteristics of NPs may be affected by the chemistry of their surroundings and the presence of inorganic and biological moieties. Consequently, understanding the behavior of NPs at the time of toxicological assay may play a crucial role in the interpretation of its results. The present study examines changes in properties of differently functionalized fluorescent 50 nm silica NPs in a variety of environments and assesses their ability to absorb proteins from cell culture medium containing either bovine or human serum. Methods: The colloidal stability depending on surface functionalization of NPs, their concentration and time of exposure was investigated in water, standard biological buffers, and cell culture media by dynamic light scattering (DLS), zeta potential measurements and transmission electron microscopy (TEM). Interactions of the particles with biological media were investigated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) in bovine and human serum, and extracted proteins were assessed using matrix-assisted laser desorption/ionization-time of flight technique (MALDI-TOF). Results: It was recognized that all of the studied silica NPs tended to agglomerate after relatively short time in buffers and biological media. The agglomeration depended not only on the NPs functionalization but also on their concentration and the incubation time. Agglomeration was much diminished in a medium containing serum. The protein corona formation depended on time and functionalization of NP, and varied significantly in different types of serum. Conclusions: Surface charge, ionic strength and biological molecules alter the properties of silica NPs and potentially affect their biological effects. The NPs surface in bovine serum and in human serum varies significantly, and it changes with incubation time. Consequently, the human serum, rather than the animal serum, should be used while conducting in vitro or in vivo studies concerning humans. Moreover, there is a need to pre-incubate NPs in the serum to control the composition of the bio-nano-composite that would be present in the human body.

Journal ArticleDOI
TL;DR: Results of UV-vis and fluorescence spectroscopies illustrated that BSA fluorescence was quenched by eupatorin via a static quenching mechanism and hydrophobic and electrostatic interactions played major roles in the interaction.
Abstract: 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.

Journal ArticleDOI
TL;DR: In this paper, three different spherical, rod and fibrous morphologies of hydroxyapatite (HA) nanoparticles have been prepared through control over the processing parameters like temperature, pH and Ca:P ratio.

Journal ArticleDOI
Lianzhi Li1, Qiong Guo1, Jianfang Dong1, Tao Xu1, Jinghong Li1 
TL;DR: Results showed that the Cu(II) complex could quench the intrinsic fluorescence of bovine serum albumin (BSA) remarkably through a static quenching process, and induce a conformational change with the loss of helical stability of protein.
Abstract: The DNA-binding properties and DNA-cleavage activities of a Cu(II) complex, [Cu(sal-tau(phen)]·1.5H2O (sal-tau=a Schiff base derived from salicylaldehyde and taurine, phen=1,10-phenanthroline), have been investigated by using UV-Vis absorption, fluorescence, circular dichroism (CD) spectra and agarose gel electrophoresis. Results indicated that this Cu(II) complex can bind to calf thymus DNA (CT-DNA) via an intercalative mode and shows efficient cleavage activity in the absence and presence of reducer. Its intrinsic binding constant Kb (1.66×10(4)M(-1)) was calculated by absorption spectra and its linear Stern-Volmer quenching constant K(sq) (3.05) was obtained from florescence spectroscopy, as well as the cleaving reaction rate constant k1 (2.0×10(-4)s(-1)) was acquired from agarose gel electrophoresis. Meanwhile, the interactions of the complex with BSA have also been studied by spectroscopy. Results showed that the complex could quench the intrinsic fluorescence of bovine serum albumin (BSA) remarkably through a static quenching process, and induce a conformational change with the loss of helical stability of protein.

Journal ArticleDOI
TL;DR: It is conclusively proved that there is a marginal structural gain of the native protein at low surfactant concentration and β-CD also induces a marginalStructural loss to the nativeprotein.
Abstract: The mechanism by which the protein bovine serum albumin undergoes unfolding induced by the anionic surfactant sodium dodecyl sulphate (SDS) and then the subsequent refolding brought in by β-Cyclodextrin (β-CD) was studied by steady-state fluorescence, time resolved measurements and Circular Dichroism (CD) spectroscopy. The prominent findings of this investigation are (i) SDS unfolds the protein in a sequential manner passing through three different phases of binding of SDS followed by a saturation phase; (ii) the refolding process is initiated through inclusion/removal of SDS molecules by β-CD and hence this also seems to happen in a phased manner; (iii) the process of refolding seems to be reversible to the unfolding process but the protein does not regain all its structure on refolding; (iv) however, CD results reveal almost 100% recovery of the secondary structure lost during SDS induced unfolding. We have conclusively proved that there is a marginal structural gain of the native protein at low surfactant concentration and β-CD also induces a marginal structural loss to the native protein. The unfolding process induced by SDS seems to be spontaneous and the binding of SDS to BSA is rather strong, as revealed by thermodynamic parameters.

Journal ArticleDOI
TL;DR: Brownian dynamics simulations show that the excluded volume and the shape of the crowding protein have a significantly stronger influence on translational and rotational diffusion coefficients, as well as transient oligomerization, than hydrodynamic or direct interactions.

Journal ArticleDOI
Xin-Yu Zhao1, Ying-Jie Zhu1, Feng Chen1, Bing-Qiang Lu1, Jin Wu1 
TL;DR: In this paper, a surfactant-free rapid microwave-assisted hydrothermal synthesis of hydroxyapatite nanosheet-assembled flower-like hierarchical nanostructures (NFHNs) is reported.
Abstract: In this paper, a surfactant-free rapid microwave-assisted hydrothermal synthesis of hydroxyapatite nanosheet-assembled flower-like hierarchical nanostructures (NFHNs) is reported. The effects of the experimental conditions on the morphology and crystal phase of the product are investigated. A possible formation mechanism of hydroxyapatite NFHNs is proposed. The morphology of the product can vary from flower-like to polyhedra by adjusting the microwave heating temperature. The protein and DNA adsorption properties of the as-prepared hydroxyapatite NFHNs are studied. The loading capacities of the as-prepared hydroxyapatite NFHNs for bovine serum albumin (BSA), hemoglobin (Hb) and fish sperm DNA are determined to be 165, 164 and 112 mg g−1, respectively. The protein release process is conducted at different pH values (pH 7.2, 5.5 and 4.8) in phosphate buffer saline (PBS), and the pH-controlled protein release behavior has been found. Thus, the as-prepared hydroxyapatite NFHNs are promising for protein drug delivery applications.

Journal ArticleDOI
TL;DR: The results of synchronous fluorescence, 3D fluorescence and FT-IR spectra show that the conformation of proteins has altered in the presence of tetrandrine, and the binding of TETD-HSA was strongly relied on the hydrophobic interaction.

Journal ArticleDOI
TL;DR: Forescence resonance energy transfer (FRET) analysis proved high probability of energy transfer from Trp residue to the drug molecule and alterations of protein secondary structure in the presence of gemcitabine were assessed by CD UV-vis and FT-IR spectroscopy.

Journal ArticleDOI
TL;DR: In this article, the authors investigated the effect of monovalent Na+ and divalent Ca2+ on UF membrane fouling behavior of different NOM fractions (humic substances, proteins, polysaccharides, as represented by humic acid (HA), bovine serum albumin (BSA), and dextran (DEX), respectively.

Journal ArticleDOI
TL;DR: IFA might be a new promising anti-glycation agent for the prevention of diabetic complications via inhibition of AGEs formation and oxidation-dependent protein damage.
Abstract: The inhibitory activity of isoferulic acid (IFA) on fructose- and glucose-mediated protein glycation and oxidation of bovine serum albumin (BSA) was investigated. Our data showed that IFA (1.25–5 mM) inhibited the formation of fluorescent advanced glycation end products (AGEs) and non-fluorescent AGE [Ne-(carboxymethyl) lysine: CML], as well as the level of fructosamine. IFA also prevented protein oxidation of BSA indicated by decreasing protein carbonyl formation and protein thiol modification. Furthermore, IFA suppressed the formation of β-cross amyloid structures of BSA. Therefore, IFA might be a new promising anti-glycation agent for the prevention of diabetic complications via inhibition of AGEs formation and oxidation-dependent protein damage.

Journal ArticleDOI
TL;DR: Two crystal structures of the complexes of equine and bovine serum albumins with 3,5-diiodosalicylic acid (DIS) are presented and results with the HSA binding ability of DIS and other structurally similar ligands are compared.

Journal ArticleDOI
TL;DR: The binding characteristics of both the serum albumins with surfactants, lipids and vesicles, polymers and dendrimers, nanomaterials and drugs and the effect of various chemical and physical denaturants on these albumins are summarized with a special emphasis on protein unfolding and refolding dynamics.

Journal ArticleDOI
TL;DR: This paper presents an overview of antitumor activity of caseins and whey proteins and derived peptides, and focuses on the ability of these molecules to provide a prevention against the development of cancer.
Abstract: Bovine milk possesses a protein system constituted by two major families of proteins: caseins (insoluble) and whey proteins (soluble). Caseins (αS1, αS2, β, and κ) are the predominant phosphoproteins in the milk of ruminants, accounting for about 80% of total protein, while the whey proteins, representing approximately 20% of milk protein fraction, include β-lactoglobulin, α-lactalbumin, immunoglobulins, bovine serum albumin, bovine lactoferrin, and lactoperoxidase, together with other minor components. Different bioactivities have been associated with these proteins. In many cases, caseins and whey proteins act as precursors of bioactive peptides that are released, in the body, by enzymatic proteolysis during gastrointestinal digestion or during food processing. The biologically active peptides are of particular interest in food science and nutrition because they have been shown to play physiological roles, including opioid-like features, as well as immunomodulant, antihypertensive, antimicrobial, antiviral, and antioxidant activities. In recent years, research has focused its attention on the ability of these molecules to provide a prevention against the development of cancer. This paper presents an overview of antitumor activity of caseins and whey proteins and derived peptides.

Journal ArticleDOI
TL;DR: Cationic bovine serum albumin-conjugated tanshinone IIA PEGylated nanoparticles possessed remarkable neuroprotective effects on ischemic stroke through modulation of inflammatory cascades and neuronal signal pathways involved in cerebral ischemia.

Journal ArticleDOI
TL;DR: Results implied that the nanoparticles possessed fine physicochemical characteristics and seemed to be a stable delivery system for poorly soluble oridonin.

Journal ArticleDOI
TL;DR: The chromatographic evaluation of the materials packed in HPLC columns showed that the HSA imprinted polydopamine offers good mechanical stability and retains practically all the target protein from an HSA solution or human plasma.

Journal ArticleDOI
TL;DR: 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.

Journal ArticleDOI
TL;DR: In this paper, a combined kinetic and mass transfer constrained protein adsorption model was proposed to get the kinetic rate constants, mass transfer coefficient, and spreading of adsorbed proteins.
Abstract: We have studied kinetics of adsorption and properties of adsorbed bovine serum albumin (BSA) and fibrinogen (Fb) on a hydrophobic octyl surface, a hydrophilic amine surface, and a mixture of octyl and amine self-assembled monolayer (SAM) and newly synthesized hybrid SAM by using quartz crystal microbalance (QCM). In addition, we have proposed a combined kinetic and mass transfer constrained protein adsorption model. The model is fitted to a change in resonance frequency, ΔFn/n versus time data obtained from QCM to get the kinetic rate constants, mass transfer coefficient, and spreading of adsorbed proteins. Initial rate of adsorption increases with a decrease in surface energy of the substrate. The equilibrium adsorbed amount of BSA on the hybrid surface is less than that on the mixed surface and lies in between that on octyl and amine surfaces and that of Fb is the least on hybrid surface. The analysis of variation of the dissipation factor, ΔD, with ΔFn/n indicates that BSA is more flexible than Fb and ...