Showing papers on "Bovine serum albumin published in 2019"
TL;DR: By focusing on recent developments made in the last two decades in BSA biosensing and determination methods, the use of different biomaterials/nanomaterials is discussed and different characteristics of BSA are highlighted.
117 citations
TL;DR: In this paper, the binding behaviors of metal ions with bovine serum albumin (BSA) were screened by using FT-IR spectroscopy, and the interaction was demonstrated by a significant reduction in the spectral intensities of the amide I (C=O stretching) and amide II bands (C−N stretching coupled to NH bending) of the protein after complexation with metal ions.
Abstract: Proteins play crucial roles in the transportation and distribution of therapeutic substances, including metal ions in living systems. Some metal ions can strongly associate, while others show low affinity towards proteins. Consequently, in the present work, the binding behaviors of Ca2+, Ba2+, Ag+, Ru3+, Cu2+ and Co2+ with bovine serum albumin (BSA) were screened. BSA and the metal ions were allowed to interact at physiological pH and their binding interactions were screened by using FT-IR spectroscopy. Spectra were collected by using hydrated films over a range of 4000–400 cm−1. The interaction was demonstrated by a significant reduction in the spectral intensities of the amide I (C=O stretching) and amide II bands (C–N stretching coupled to NH bending) of the protein after complexation with metal ions. The binding interaction was further revealed by spectral shifting of the amide I band from 1651 cm−1 (free BSA) to 1653, 1654, 1649, 1655, 1655, and 1654 cm−1 for BSA–Ca2+, BSA–Ba2+, BSA–Ag+, BSA–Ru3+, BSA–Cu2+ and BSA–Co2+ complexes, respectively. The shifting of the amide I band was due to the interactions of metal ions with the O and N atoms of the ligand protein. Estimation of the secondary protein structure showed alteration in the protein conformation, characterized by a marked decrease (12.9–40.3%) in the α-helix accompanied by increased β-sheet and β-turn after interaction with the metal ions. The interaction results of this study were comparable with those reported in our previous investigation of metal ion–BSA interactions using affinity capillary electrophoresis (ACE), which has proven the accuracy of the FT-IR technique in the measurement of interactions between proteins and metal ions.
103 citations
TL;DR: Binding study of triamcinolone with BSA through in vitro and in silico approaches, helping in the development of drugs with better therapeutic efficacy.
Abstract: The biomolecular interaction of triamcinolone with bovine serum albumin (BSA) was studied using various multi-spectroscopic techniques in combination with in silico studies. UV-visible absorption, fluorescence spectroscopy and resonance Rayleigh scattering studies confirmed the formation of a BSA–triamcinolone complex. The binding constant was found to be in the order of 103 M−1. Conformational and microenvironmental changes in BSA after addition of triamcinolone were confirmed by circular dichroism and 3D fluorescence spectroscopy, respectively. The negative values of ΔG and ΔH confirmed spontaneous and exothermic binding. The average binding distance between BSA and triamcinolone was also calculated through FRET. Additionally, the effect of metal ions and β-cyclodextrin on the binding of triamcinolone with BSA was also investigated. Molecular docking and site marker displacement experiments unveiled the binding of triamcinolone to BSA at site III located in subdomain IB of BSA. Molecular dynamics simulation showed lower RMSD values and negative total energy, suggesting favourable binding between BSA and triamcinolone.
63 citations
TL;DR: Docking results revealed β-C was bound to the subdomain IIA of BSA, the residues of aromatic cluster II in α-lactalbumin and into the calyx of β- lactoglobulin resulting in conformational changes in the secondary and tertiary structures of proteins.
62 citations
TL;DR: Examination of the interaction between Repaglinide and a model protein, bovine serum albumin, employing various spectroscopic, electrochemical and molecular docking methods revealed that RPG quenched the intensity of BSA through dynamic quenching mechanism.
62 citations
TL;DR: This first standardized investigation of the influence of different media supplements on NET formation in vitro shows that mouse and human neutrophils have different susceptibilities toward the inhibition of NETosis by albumin or serum components, and provides experimental evidence that albumin inhibitsNETosis by scavenging activators such as LPS.
Abstract: The formation of neutrophil extracellular traps (NETs) is an immune defense mechanism of neutrophilic granulocytes. Moreover, it is also involved in the pathogenesis of autoimmune, inflammatory, and neoplastic diseases. For that reason, the process of NET formation (NETosis) is subject of intense ongoing research. In vitro approaches to quantify NET formation are commonly used and involve neutrophil stimulation with various activators such as phorbol 12-myristate 13-acetate (PMA), lipopolysaccharides (LPS), or calcium ionophores (CaI). However, the experimental conditions of these experiments, particularly the media and media supplements employed by different research groups, vary considerably, rendering comparisons of results difficult. Here, we present the first standardized investigation of the influence of different media supplements on NET formation in vitro. The addition of heat-inactivated (hi) fetal calf serum (FCS), 0.5% human serum albumin (HSA), or 0.5% bovine serum albumin (BSA) efficiently prevented NET formation of human neutrophils following stimulation with LPS and CaI, but not after stimulation with PMA. Thus, serum components such as HSA, BSA and hiFCS (at concentrations typically found in the literature) inhibit NET formation to different degrees, depending on the NETosis inducer used. In contrast, in murine neutrophils, NETosis was inhibited by FCS and BSA, regardless of the inducer employed. This shows that mouse and human neutrophils have different susceptibilities toward the inhibition of NETosis by albumin or serum components. Furthermore, we provide experimental evidence that albumin inhibits NETosis by scavenging activators such as LPS. We also put our results into the context of media supplements most commonly used in NET research. In experiments with human neutrophils, either FCS (0.5-10%), heat-inactivated (hiFCS, 0.1-10%) or human serum albumin (HSA, 0.05-2%) was commonly added to the medium. For murine neutrophils, serum-free medium was used in most cases for stimulation with LPS and CaI, reflecting the different sensitivities of human and murine neutrophils to media supplements. Thus, the choice of media supplements greatly determines the outcome of experiments on NET-formation, which must be taken into account in NETosis research.
60 citations
TL;DR: It was found that a pH shift of the immobilization medium from acidic to alkaline values is accompanied by a change in the mechanism of protein adsorption on the gold surface, leading to multilayer immobilization.
59 citations
TL;DR: In this paper, surface imprinted tubular carbon nanofibers (SIPTCFs) with self-driven property are first developed in order to promote the development of protein purification.
58 citations
TL;DR: The binding interactions between bovine serum albumin and a large excess of uric acid (UA) have been analyzed in aqueous solution at pH = 7.4, using UV-vis absorption and steady-state, time-resolved, synchronous and three-dimensional fluorescence spectra techniques.
58 citations
TL;DR: Insight is provided into possible biophysical mechanisms whereby cells can control the uptake of proteins into coacervate-like granules, and future utility in applications ranging from medicine and sensing to remediation and biocatalysis is suggested.
Abstract: We investigated the encapsulation of the model proteins bovine serum albumin (BSA), human hemoglobin (Hb), and hen egg white lysozyme (HEWL) into two-polymer complex coacervates as a function of polymer and solution conditions. Electrostatic parameters such as pH, protein net charge, salt concentration, and polymer charge density can be used to modulate protein uptake. While the use of a two-polymer coacervation system enables the encapsulation of weakly charged proteins that would otherwise require chemical modification to facilitate electrostatic complexation, we observed significantly higher uptake for proteins whose structure includes a cluster of like-charged residues on the protein surface. In addition to enhancing uptake, the presence of a charge patch also increased the sensitivity of the system to modulation by other parameters, including the length of the complexing polymers. Lastly, our results suggest that the distribution of charge on a protein surface may lead to different scaling behaviour for both the encapsulation efficiency and partition coefficient as a function of the absolute difference between the protein isoelectric point and the solution pH. These results provide insight into possible biophysical mechanisms whereby cells can control the uptake of proteins into coacervate-like granules, and suggest future utility in applications ranging from medicine and sensing to remediation and biocatalysis.
54 citations
TL;DR: It is indicated that serum proteins can transport tea catechins in vitro as well as polyphenol-protein conjugates in vitro.
TL;DR: Two dual sensing platforms based on the combination of a plasma separation pad and GOD-GO/MnO2 for direct detection of glucose concentration in whole blood by colorimetric assay without blood sample pretreatment are constructed, suggesting potential clinical applications in blood glucose monitoring for diabetic patients.
Abstract: We herein report a facile approach for the preparation of horseradish peroxidase (HRP)-mimic glucose oxidase-conjugated graphene oxide/MnO2 (GOD-GO/MnO2) as new nanozyme to detect the glucose concentration in whole blood. The nano-sized of MnO2 nanoparticles embedded in bovine serum albumin (BSA)-coated GO by in situ growth were evaluated focusing on the principle of HRP-mimic activity catalyzing the oxidation of 3,3',5,5'-tetramethylbenzidine (TMB) in the presence of hydrogen peroxide. Furthermore, we constructed dual sensing platforms based on the combination of a plasma separation pad and GOD-GO/MnO2 for direct detection of glucose concentration in whole blood by colorimetric assay without blood sample pretreatment. As a proof-of-concept, a limit of detection of 3.1 mg dL-1 for glucose was obtained with a wide linear quantification range from 25 mg dL-1 to 300 mg dL-1 through visual observation and quantitative analysis, suggesting potential clinical applications in blood glucose monitoring for diabetic patients.
TL;DR: Results indicated that the chitosan-based membrane prepared in this work had great potential for pretreatment of samples in glycoproteomics.
Abstract: In the study of glycoproteomics with mass spectrometry, certain pretreatments of samples are required for eliminating the interference of nonglycopeptides and improving the efficiency of glycopeptides detection. Although hydrophilic interaction chromatography (HILIC) has been developed for enrichment of glycosylated peptides, a plethora of hydrophilic materials always suffered from large steric hindrance, great cost, and difficulty with modifications of high-density hydrophilic groups. In this work, a 1 mm thick biomimetic honeycomb chitosan membrane (BHCM) with honeycomb-like accessible macropores was directly prepared by the freeze-casting method as an adsorbent for HILIC. The N-glycopeptides from trypsin digests of immunoglobulin G (IgG), mixture of IgG and bovine serum albumin (BSA), and serum proteins were enriched using this material and compared with a commercial material ZIC-HILIC. The biomimetic membrane could identify as many as 32 N-glycopeptides from the IgG digest, exhibiting high sensitivity...
TL;DR: Analysis of biomarker candidates in serum/plasma samples frequently requires separation of their components, usually including depletion of albumin in a fraction of interest, which is critical in proteomic analysis based on mass spectrometry.
Abstract: Blood serum or plasma proteome is a gold mine of disease biomarkers. However, complexity and a huge dynamic range of their components, combined with multiple mechanisms of degradation and posttranslational modifications, further complicated by the presence of lipids, salts, and other metabolites, represent a real challenge for analytical sensitivity, resolution, and reproducibility. This problem exists particularly in the case of potential disease-specific markers, most typically represented by low-abundant proteins (LAPs), whose detection is usually impaired by the dominance of albumins, immunoglobulins, and other high-abundant serum/plasma proteins (HAPs). Hence, analysis of biomarker candidates in serum/plasma samples frequently requires separation of their components, usually including depletion of albumin in a fraction of interest. Such “preprocessing” of serum/plasma specimens is critical in proteomic analysis based on mass spectrometry. This approach is very potent; nevertheless a wide range of protein concentrations in serum/plasma represents a particular challenge, since high-abundant proteins (mostly albumin) dominate in a sample subjected to mass spectrometry and suppress peptide ions originating from low-abundant proteins, thus limiting probability and reliability of their detection. An emerging approach in serum-/plasma-based biomarker-oriented studies is the proteome component of exosomes – nanovesicles secreted by cells and involved in multiple aspects of intercellular communication. However, the presence of albumin, frequent contaminant of exosomes isolated from human serum/plasma, represents a real challenge also in this type of study. A similar problem is encountered in proteomic studies based on exosomes obtained in in vitro experiments where culture media are normally supplemented with fetal bovine serum containing growth factors and hormones. In this case exosomes are frequently contaminated with bovine serum albumin and other bovine serum proteins which should be removed before proteomic analysis of exosome cargo.
TL;DR: It is shown that BSA could protect blueberry anthocyanins against degradation and retain their antioxidant activity at an ideal concentration of 0.15 mg/mL under three deteriorating treatments: illumination, vitamin C + illumination, and sucrose + illumination.
TL;DR: A protease-proof nano-assembly was derived from the BSA-CD conjugate through desolvation that simultaneously hosts a prototype antibiotic and generates ROS with excellent efficiency, making it an attractive platform for antibacterial Photodynamic Therapy (A-PDT) applications.
Abstract: Amplification of reactive oxygen species (ROS) generation through covalent conjugation of bovine serum albumin (BSA) with newly synthesized, ROS-producing carbon dots (CDs) upon visible light irradiation is reported for the first time. Derivatization of surface carboxyl functional groups of Anthrarufin-derived, green-emitting CD with the amine functionality of BSA ushers distinct changes in the photophysics of CD including an unprecedented ∼50 nm shift in its excitation maxima, decrease in fluorescence lifetime, and concomitant increase in ROS generation. Substantial conformational changes of BSA were witnessed upon conjugation with CD, rendering the BSA-CD conjugate resistant to pepsinolysis. A protease-proof nanoassembly was derived from the BSA-CD conjugate through desolvation that simultaneously hosts a prototype antibiotic and generates ROS with excellent efficiency, making it an attractive platform for antibacterial photodynamic therapy (A-PDT) applications. Systemic annihilation of both Gram-positive and -negative bacteria was achieved with the BSA-CD nanoassembly and envisioned as alternatives to traditional photosensitizers.
TL;DR: The B SA-GQDs based chiral sensor exhibited good biomolecular homochirality in the recognition of Trp isomers, and the higher affinity of BSA-G QDs toward L-Trp than its isomer, D-trp, was also revealed by density functional theory (DFT) considering the possible hydrogen bonds between the Tr p isomers and the solvent accessible residues of B SA.
Abstract: Stereospecific molecular recognition with simple and easily available proteins is of significant importance in life science and biomaterial science. Herein, we report on a chiral sensing platform, graphene quantum dots (GQDs)-functionalized bovine serum albumin (BSA), for chiral recognition of tryptophan (Trp) isomers. Amidation reaction between BSA and GQDs was directly responsible for the introduction of GQDs to BSA, resulting in significant changes in the spatial configuration of BSA and the exposure of more chiral sites at the protein surface. The BSA-GQDs-based chiral sensor exhibited good biomolecular homochirality in the recognition of Trp isomers, and the higher affinity of BSA-GQDs toward l-Trp than its isomer, d-Trp, was also revealed by density functional theory (DFT) considering the possible hydrogen bonds between the Trp isomers and the solvent-accessible residues of BSA.
TL;DR: The results indicate that lipid composition and concentration affect the adsorption of proteins and the liposomal stabilization, and that the protein binding depends on the presence of polyethylene glycol, CH, concentration and surface charge.
Abstract: The aim of the present study is to investigate the interactions between liposomes and proteins and to evaluate the role of liposomal lipid composition and concentration in the formation of protein corona. Liposomes composed of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) or hydrogenated soybean phosphatidylcholine (HSPC) with 1,2-dipalmitoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (sodium salt) (DPPG), 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine-N-[methoxy(polyethylene glycol)-3000] (DPPE-PEG 3000), cholesterol (CH) or mixtures of these lipids, were prepared at different concentrations by the thin-film hydration method. After liposomes were dispersed in HPLC-grade water and foetal bovine serum (FBS), their physicochemical characteristics, such as size, size distribution, and ζ-potential, were determined using dynamic and electrophoretic light scattering. Aggregation of DPPC, HSPC, DPPC:CH (9:1 molar ratio), and HSPC:CH (9:1 molar ratio) in FBS was observed. On the contrary, liposomes incorporating DPPG lipids and CH both in a molar ratio of 11% were found to be stable over time, while their size did not alter dramatically in biological medium. Liposomes containing CH and PEGylated lipids retain their size in the presence of serum as well as their physical stability. In addition, our results indicate that the protein binding depends on the presence of polyethylene glycol (PEG), CH, concentration and surface charge. In this paper, we introduce a new parameter, fraction of stealthiness (Fs), for investigating the extent of protein binding to liposomes. This parameter depends on the changes in size of liposomes after serum incubation, while liposomes have stealth properties when Fs is close to 1. Thus, we conclude that lipid composition and concentration affect the adsorption of proteins and the liposomal stabilization.
TL;DR: EGAC-BSA appears to be promising as an effective oral delivery system for proteins with enhanced intestinal absorption after oral administration in rats, significantly enhanced the intestinal permeation of BSA compared to free BSA.
TL;DR: The analysis of thermodynamic parameter revealed the involvement of hydrogen bonding and van der Waals forces in the IND-BSA interaction and suggested conformational change in BSA molecule post interaction to IND.
TL;DR: Four bichromophoric cyclometalated iridium complexes were synthesized and fully characterized and localization experiments of intracellular complexes by confocal microscopy suggested that these complexes enter cancer cells through energy dependence and specifically target the lysosomes, thus resulting in the damage of lysOSomes.
TL;DR: An efficient and novel 2,5-bis(benzo[d]thiazol-2-yl)phenol scaffold-based ratiometric fluorescent probe BTP-Cys for the sensing of cysteine has been developed and has been successfully constructed on account of the excited state intramolecular proton transfer (ESIPT) mechanism.
TL;DR: In this paper, a multi-technique approach has been used to probe the interaction of model protein bovine serum albumin (BSA) with a series of substantially biodegradable and less cytotoxic ethylene-oxide linked ester-functionalized gemini surfactants (designated as Cm-E2O-Cm, m
TL;DR: In this article, the pyrazoline pyridazine derivative 7-methyl-2-phenyl-4-(3,4,5-trimethoxyphenyl)-2H-pyrazolo[3, 4-d]pyridine (5d) was studied for its interaction with bovine serum albumin (BSA).
Abstract: In this research, the pyrazoline pyridazine derivative 7-methyl-2-phenyl-4-(3,4,5-trimethoxyphenyl)-2H-pyrazolo[3,4-d]pyridazine (5d) was studied for its interaction with bovine serum albumin (BSA). Various spectroscopic techniques along with molecular docking analysis were utilized to understand the mechanism of interaction. The quenching of BSA fluorescence by using investigational drug 5d was the basic principle for the methodology. Spectrofluorometric methods and UV-absorption studies were conducted for exploration of the 5d and BSA binding mechanism. The fluorescence quenching mechanism involved in BSA and 5d interaction was static quenching, and a complex formation also occurred between them. Both enthalpy and entropy attained positive values suggesting involvement of hydrophobic forces in BSA and 5d interaction. The Forster distance of 2.23 nm was calculated by fluorescence resonance energy transfer (FRET). An alteration in BSA secondary structure was proven from the conformational studies of BSA-5d interaction. This binding interaction study provided a basis to comprehend the binding interaction between 5d and BSA. These results provided information about sites of BSA involved in its interaction with 5d.
TL;DR: A novel poly(ionic liquid) with 1-vinyl-3-aminopropyl imidazolium cations was designed and used to modify cellulose aerogels via Schiff base reaction and exhibited a well-interconnected porous structure and a high porosity.
TL;DR: The multifunctional nano-dBSA functionalization can confer a new function to graphene-like 2D nanomaterials and provide a promising bio-functionalization method for clinical application in biosensing, nanomedicine, and drug delivery.
Abstract: A simple, convenient, and highly sensitive bio-interface for graphene field-effect transistors (GFETs) based on multifunctional nano-denatured bovine serum albumin (nano-dBSA) functionalization was developed to target cancer biomarkers. The novel graphene–protein bioelectronic interface was constructed by heating to denature native BSA on the graphene substrate surface. The formed nano-dBSA film served as the cross-linker to immobilize monoclonal antibody against carcinoembryonic antigen (anti-CEA mAb) on the graphene channel activated by EDC and Sulfo-NHS. The nano-dBSA film worked as a self-protecting layer of graphene to prevent surface contamination by lithographic processing. The improved GFET biosensor exhibited good specificity and high sensitivity toward the target at an ultralow concentration of 337.58 fg mL−1. The electrical detection of the binding of CEA followed the Hill model for ligand–receptor interaction, indicating the negative binding cooperativity between CEA and anti-CEA mAb with a dissociation constant of 6.82 × 10−10 M. The multifunctional nano-dBSA functionalization can confer a new function to graphene-like 2D nanomaterials and provide a promising bio-functionalization method for clinical application in biosensing, nanomedicine, and drug delivery.
TL;DR: The collaborative results of spectroscopic studies indicated that the microenvironment and the conformation of HSA and BSA were significantly perturbed upon interaction with complex [C36H50N8O6Cu].
Abstract: The interaction studies of CuII nalidixic acid–DACH chemotherapeutic drug entity, [C36H50N8O6Cu] with serum albumin proteins, viz., human serum albumin (HSA) and bovine serum albumin (BSA) employin...
TL;DR: FA-modified albumin nanoparticles are good carriers for delivering SRF to the tumor tissue, which can improve the therapeutic effect and reduce the side effects of the drug.
Abstract: Background: To prepare sorafenib-loaded folate-decorated bovine serum nanoparticles (FA-SRF-BSANPs) and investigate their effect on the tumor targeting.Methods: The nanoparticles were characterized...
TL;DR: The experimental data revealed that the synthesized terpolymeric semi-IPN hydrogel may have useful biomedical applications, especially as a carrier of protein (BSA), or 5-ASA (a therapeutic option for conditions of the colon such as Crohn's Disease and Ulcerative Colitis).