Showing papers on "Bovine serum albumin published in 2017"
TL;DR: The results reveal that BSA‐coating significantly improves the origami stability against endonucleases (DNase I) and enhances the transfection into human embryonic kidney (HEK293) cells and attenuates the activation of immune response in mouse primary splenocytes.
Abstract: Fully addressable DNA nanostructures, especially DNA origami, possess huge potential to serve as inherently biocompatible and versatile molecular platforms. However, their use as delivery vehicles in therapeutics is compromised by their low stability and poor transfection rates. This study shows that DNA origami can be coated by precisely defined one-to-one protein-dendron conjugates to tackle the aforementioned issues. The dendron part of the conjugate serves as a cationic binding domain that attaches to the negatively charged DNA origami surface via electrostatic interactions. The protein is attached to dendron through cysteine-maleimide bond, making the modular approach highly versatile. This work demonstrates the coating using two different proteins: bovine serum albumin (BSA) and class II hydrophobin (HFBI). The results reveal that BSA-coating significantly improves the origami stability against endonucleases (DNase I) and enhances the transfection into human embryonic kidney (HEK293) cells. Importantly, it is observed that BSA-coating attenuates the activation of immune response in mouse primary splenocytes. Serum albumin is the most abundant protein in the blood with a long circulation half-life and has already found clinically approved applications in drug delivery. It is therefore envisioned that the proposed system can open up further opportunities to tune the properties of DNA nanostructures in biological environment, and enable their use in various delivery applications.
160 citations
TL;DR: Transduction of apoptotic proteins and peptides successfully induces apoptosis in cancer cells, suggesting that the activities of proteins and Peptides are maintained during the delivery.
Abstract: The efficient delivery of biopharmaceutical drugs such as proteins and peptides into the cytosol of target cells poses substantial challenges owing to their large size and susceptibility to degradation. Current protein delivery vehicles have limitations such as the need for protein modification, insufficient delivery of large-size proteins or small peptides, and loss of protein function after the delivery. Here, we adopted a rational approach to design a polymer with robust efficacy for intracellular protein and peptide delivery. The polymer is composed of a dendrimer scaffold, a hydrophobic membrane-disruptive region, and a multivalent protein binding surface. It allows efficient protein/peptide binding, endocytosis, and endosomal disruption and is capable of efficiently delivering various biomacromolecules including bovine serum albumin, R-phycoerythrin, p53, saporin, β-galactosidase, and peptides into the cytosol of living cells. Transduction of apoptotic proteins and peptides successfully induces apop...
146 citations
TL;DR: Estazolam (Figure S1(a), is one of the representative of the triazolobenzodiazepine drugs that acts on the central nervous system, mainly prescribed as a sedative and hypnotic agent.
Abstract: Estazolam (Figure S1(a)), is one of the representative of the triazolobenzodiazepine drugs that acts on the central nervous system, mainly prescribed as a sedative and hypnotic agent (Lee et al., 2...
112 citations
TL;DR: A new protein nanocarrier made of graphene oxide (GO) + Chitosan (CS) is proposed to successfully prevent proteolysis in protein and simultaneously retain its activity.
Abstract: Proteins have short half-life because of enzymatic cleavage. Here, a new protein nanocarrier made of graphene oxide (GO) + Chitosan (CS) is proposed to successfully prevent proteolysis in protein and simultaneously retain its activity. Bovine serum albumin (BSA) and collagenase were loaded on GO and GO-CS to explore the stability and activity of proteins. SEM, AFM, TEM, DSC, UV-Vis, FT-IR, RBS, Raman, SDS-PAGE and zymography were utilized as characterization techniques. The protecting role of GO and GO-CS against enzymatic cleavage was probed by protease digestion analysis on BSA, where the protease solution was introduced to GO-BSA and GO-CS-BSA at 37 °C for 0.5-1-3-6 hours. Characterizations showed the successful synthesis of few layers of GO and the coverage by CS. According to gelatin zymographic analysis, the loaded collagenase on GO and GO-CS lysed the gelatin and created non-staining bands which confirmed the activity of loaded collagenase. SDS-PAGE analysis revealed no significant change in the intact protein in the GO-BSA and GO-CS-BSA solution after 30-minute and 1-hour exposure to protease; however, free BSA was completely digested after 1 hour. After 6 hours, intact proteins were detected in GO-BSA and GO-CS-BSA solutions, while no intact protein was detected in the free BSA solution.
108 citations
TL;DR: In this article, the protein-ligand interaction mechanisms can help to better construct the nanocarrier to delivery fucoxanthin, and the results indicated that the skeletons of BSA/β-Lg/α-La were loosened and unfolded and the protein aggregates were formed with a nano scale.
107 citations
TL;DR: This work paves a new way for fast functionalization of MOF and also provides a novel idea for material design in sample preparation, especially in glycoproteome and related analysis.
Abstract: Cysteine-functionalized metal–organic framework (MOF) was synthesized via a common and facile two-step method of in situ loading of Au nanoparticles on amino-derived MOF followed by l-cysteine (Cys) immobilization Owing to the large specific surface area and ultrahigh hydrophilicity of this nanocomposite, excellent performance was observed in the enrichment of N-linked glycopeptides in both model glycoprotein and HeLa cell lysate By using this nanocomposite, 16 and 31 glycopeptides were efficiently extracted from digest of horseradish peroxidase (HRP) and human serum immunoglobulin G (IgG), respectively The short incubation time (5 min), large binding capacity (150 mg/g, IgG digest to material), good selectivity (1:50, molar ratio of IgG and bovine serum albumin (BSA) digest), high recovery (over 80%), and low detection limit (1 fmol) ensure the effectiveness and robustness of MIL-101(NH2)@Au-Cys in complex HeLa cell lysate As a result, 1123 N-glycosylation sites corresponding to 1069 N-glycopeptides
106 citations
01 May 2017
TL;DR: Differences in protein structure and protein adsorption at acidic pH highlight for the first time the extent to which the protein corona structure is significantly impacted by protein-nanoparticle interactions which depend on the interplay between pH and specific nanoparticle surface chemistry.
Abstract: The interaction of a model protein, bovine serum albumin (BSA) with two different metal oxide nanoparticles, TiO2 (∼22 nm) and SiO2 (∼14 nm), was studied at both physiological and acidic pH. The pH- and nanoparticle-dependent differences in protein structure and protein adsorption were determined using attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR) and thermogravimetric analysis (TGA). The results indicated that the surface coverage of BSA decreases with decreasing pH on both TiO2 and SiO2 surfaces, and BSA coverage is higher by a factor of ca. 3–10 times more on TiO2 compared to SiO2. The secondary structure of BSA changes upon adsorption to either nanoparticle surface at both pH 7.4 and 2. At acidic pH, BSA appears to completely unfold on TiO2 nanoparticles whereas it assumes an extended conformation on SiO2. These differences highlight for the first time the extent to which the protein corona structure is significantly impacted by protein-nanoparticle interactions which depend on the interplay between pH and specific nanoparticle surface chemistry.
99 citations
TL;DR: The quenching interaction of atomoxetine (ATX) with bovine serum albumin (BSA) was studied in vitro under optimal physiological condition by multi-spectroscopic techniques and indicated that intermolecular hydrophobic forces predominantly stabilized the drug-protein system.
97 citations
TL;DR: A point-of-care sensor for the detection of folic acid protein (FAP) using graphene-based SPR chips that allowed femtomolar (fM) detection of FAP, a detection limit well adapted and promising for quantitative clinical analysis.
96 citations
TL;DR: Results showed that MH was more effective on the reduction of free amino groups and increase in absorbance at 420nm more than CH (p<0.05) and higher values in solubility, emulsion activity and foam capacity were obtained during MH heating which could be attributed to different structural changes of proteins under MH and CH.
85 citations
TL;DR: A novel sandwich strategy was designed to detect Staphylococcus aureus based on an antibacterial agent that captures bacterial cells and a fluorescein-labeled antibody that acts as the signal-output probe and showed ideal specificity.
Abstract: A novel sandwich strategy was designed to detect Staphylococcus aureus. The strategy is based on an antibacterial agent that captures bacterial cells and a fluorescein-labeled antibody that acts as the signal-output probe. Vancomycin (Van), which exerts a strong antibacterial effect on Gram-positive bacteria, was utilized as a molecular recognition agent to detect pathogenic bacteria. To effectively concentrate S. aureus, we used bovine serum albumin (BSA) as the amplification carrier to modify magnetic beads (MBs), which were then functionalized with Van. To improve the specificity of the method for S. aureus detection, we adopted fluorescein isothiocyanate (FITC)-tagged pig immunoglobulin G (FITC-pig IgG) as the signal probe and the second recognition agent that bound between the Fc fragment of pig IgG and protein A in the surface of S. aureus. To quantify S. aureus, we measured the fluorescence signal by flow cytometry (FCM). The use of multivalent magnetic nanoprobes (Van-BSA-MBs) showed a high concen...
TL;DR: Lysozyme and bovine serum albumin have been investigated by means of circular dichroism and small-angle neutron scattering and results towards understanding protein conformation in choline chloride-based DES and mixtures with water are presented.
Abstract: Deep eutectic solvents (DES) have recently been postulated as possible environments where protein structure may be preserved in the absence of water. Here we present our results towards understanding protein conformation in choline chloride-based DES and mixtures with water. Lysozyme and bovine serum albumin have been investigated by means of circular dichroism and small-angle neutron scattering.
TL;DR: 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 foulingresistant ability, suggesting superior antifouling performance.
TL;DR: In this article, a ratiometric fluorescence biosensor was developed for detection of double strand DNA (dsDNA), which consists of water-soluble fluorescent carbon dots (CDs) and 3-mercapropionic acid-coated cadmium telluride (CdTe) quantum dots exhibiting emissions peaks at 435 and 599 nm under single-wavelength excitation (360 nm).
Abstract: A ratiometric fluorescence biosensor was developed for detection of double strand DNA (dsDNA). The sensor consists of water-soluble fluorescent carbon dots (CDs) and 3-mercapropionic acid-coated cadmium telluride (CdTe) quantum dots exhibiting emissions peaks at 435 and 599 nm, respectively, under single-wavelength excitation (360 nm). CdTe QDs fluorescence was quenched by mitoxantrone via electron transfer and was restored in the presence of dsDNA, while the fluorescence intensity of CDs remained almost constant, providing a ratiometric means of dsDNA detection. The relative fluorescence intensity ration is directly proportional to the concentration of dsDNA between 0 and 50 nM, and the detection limit is 1.0 nM. Meanwhile, common organic compounds including amino acids, nucleotides, bovine serum albumin, single strand DNA and RNA had not significant interference in the detection mode. The novel nanosensor is simple, rapid, and convenient since it does not require modification or separation procedures, and was applied to the detection of HIV dsDNA in synthetic samples and human serum samples with satisfactory results.
TL;DR: Seven novel half-sandwich IrIII cyclopentadienyl complexes, [(η5-Cpx)Ir(N^N)Cl]PF6, have been prepared and characterized, and most of the complexes show potent antiproliferative activity towards A549 and HeLa cancer cells, except for Cp* complex 1A towards HeLa cells.
Abstract: Seven novel half-sandwich IrIII cyclopentadienyl complexes, [(η5-Cpx)Ir(N^N)Cl]PF6, have been prepared and characterized, where Cpx is Cp* or the biphenyl derivative Cpxbiph (C5Me4C6H4C6H5), and the N^N-chelating ligands are imino-pyridyl Schiff-bases. The X-ray crystal structures of complexes 2A, 2B, and 3A have been determined. Excitingly, most of the complexes show potent antiproliferative activity towards A549 and HeLa cancer cells, except for Cp* complex 1A towards HeLa cells. Cpxbiph complex 2B displayed the highest potency, about 19 and 6 times more active than the clinically used drug cisplatin toward A549 and HeLa cells, respectively. These complexes undergo hydrolysis, and the kinetics data have been calculated. DNA binding has been studied by interaction with nucleobases 9-ethylguanine and 9-methyladenine, cleavage of plasmid DNA, and interaction with ctDNA. Interaction with DNA does not appear to be the major mechanism of action. Protein binding (bovine serum albumin, BSA) has been established by UV-Vis, fluorescence and synchronous spectroscopic studies. The stability of complex 2B in the presence of GSH was evaluated. The complexes catalytically convert coenzyme NADH to NAD+via hydride transfer. Cpxbiph complexes 2B and 4B induce cell apoptosis and arrest cell cycles at the S and G2/M phases towards A549 cancer cells and increase the reactive oxygen species dramatically, which appear to contribute to the remarkable anticancer activity.
TL;DR: This study presents a novel approach based on a four-electrode electrochemical biosensor for the detection of tau protein - one of the possible markers for the prediction of Alzheimer's disease (AD).
TL;DR: Tannic acid shows strong interactions with proteins and the resulting complexes can be utilized as delivery systems for oral drugs, and it is suggested that BLG-TA is the most stable complex.
TL;DR: It is demonstrated that microcapsules released Lf in small intestine allowing 6.5 times higher concentration than in control group dosed with the same amount of free Lf.
Abstract: Lactoferrin (Lf) has considerable potential as a functional ingredient in food, cosmetic and pharmaceutical applications. However, the bioavailability of Lf is limited as it is susceptible to digestive enzymes in gastrointestinal tract. The shells comprising alternate layers of bovine serum albumin (BSA) and tannic acid (TA) were tested as Lf encapsulation system for oral administration. Lf absorption by freshly prepared porous 3 μm CaCO3 particles followed by Layer-by-Layer assembly of the BSA-TA shells and dissolution of the CaCO3 cores was suggested as the most efficient and harmless Lf loading method. The microcapsules showed high stability in gastric conditions and effectively protected encapsulated proteins from digestion. Protective efficiency was found to be 76 ± 6% and 85 ± 2%, for (BSA-TA)4 and (BSA-TA)8 shells, respectively. The transit of Lf along the gastrointestinal tract (GIT) of mice was followed in vivo and ex vivo using NIR luminescence. We have demonstrated that microcapsules released Lf in small intestine allowing 6.5 times higher concentration than in control group dosed with the same amount of free Lf. Significant amounts of Lf released from microcapsules were then absorbed into bloodstream and accumulated in liver. Suggested encapsulation system has a great potential for functional foods providing lactoferrin.
TL;DR: The experimental results showed that SIM, PRA, FLU, and PIT statins quenched the intrinsic fluorescence of BSA through a static quenching process and the stable stains–BSA complexes with the binding constants in the order of 104 M−1 at 298 K were formed through intermolecular nonbond interaction.
Abstract: The binding interactions of simvastatin (SIM), pravastatin (PRA), fluvastatin (FLU), and pitavastatin (PIT) with bovine serum albumin (BSA) were investigated for determining the affinity of four statins with BSA through multiple spectroscopic and molecular docking methods. The experimental results showed that SIM, PRA, FLU, and PIT statins quenched the intrinsic fluorescence of BSA through a static quenching process and the stable stains-BSA complexes with the binding constants in the order of 104 M-1 at 298 K were formed through intermolecular nonbond interaction. The values of ΔH0, ΔS0 and ΔG0 in the binding process of SIM, PRA, FLU, and PIT with BSA were negative at the studied temperature range, suggesting that the binding process of four statins and BSA was spontaneous and the main interaction forces were van der Waals force and hydrogen-bonding interactions. Moreover, the binding of four statins with BSA was enthalpy-driven process due to |ΔH°|>|TΔS°| under the studied temperature range. From the results of site marker competitive experiments and molecular docking, subdomain IIIA (site II) was the primary binding site for SIM, PRA, FLU, and PIT on BSA. The results of UV-vis absorption, synchronous fluorescence, 3D fluorescence and FT-IR spectra proved that the slight change in the conformation of BSA, while the significant changes in the conformation of SIM, PRA, FLU, and PIT drug in statin-BSA complexes, indicating that the flexibility of statin molecules plays an important role in increasing the stability of statin-BSA complexes.
TL;DR: 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 B SA through a static quenching process, implying that the flexibility of clonZepam also played an important role in increasing the stability of the clonAZepam-BSA complex.
Abstract: 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 (Kb) of clonazepam-BSA complex were about 1 and 7.94 × 104 M− 1 at 308 K, respectively. The binding process of clonazepam with BSA was spontaneous and enthalpy-driven process due to ΔG0 T | ΔS0 | 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.
TL;DR: Evidence is observed for a site-selective formation of free amino acids in the OH radical-induced oxidation of peptides and proteins, which may be due to a reaction pathway involving nitrogen-centered radicals.
Abstract: Hydroxyl radical-induced oxidation of proteins and peptides can lead to the cleavage of the peptide, leading to a release of fragments. Here, we used high-performance liquid chromatography tandem mass spectrometry (HPLC-MS/MS) and pre-column online ortho-phthalaldehyde (OPA) derivatization-based amino acid analysis by HPLC with diode array detection and fluorescence detection to identify and quantify free amino acids released upon oxidation of proteins and peptides by hydroxyl radicals. Bovine serum albumin (BSA), ovalbumin (OVA) as model proteins, and synthetic tripeptides (comprised of varying compositions of the amino acids Gly, Ala, Ser, and Met) were used for reactions with hydroxyl radicals, which were generated by the Fenton reaction of iron ions and hydrogen peroxide. The molar yields of free glycine, aspartic acid, asparagine, and alanine per peptide or protein varied between 4 and 55%. For protein oxidation reactions, the molar yields of Gly (∼32-55% for BSA, ∼10-21% for OVA) were substantially higher than those for the other identified amino acids (∼5-12% for BSA, ∼4-6% for OVA). Upon oxidation of tripeptides with Gly in C-terminal, mid-chain, or N-terminal positions, Gly was preferentially released when it was located at the C-terminal site. Overall, we observe evidence for a site-selective formation of free amino acids in the OH radical-induced oxidation of peptides and proteins, which may be due to a reaction pathway involving nitrogen-centered radicals.
TL;DR: In this paper, the van der Waals force and hydrogen bonding were the main intermolecular forces stabilizing the complex in a spontaneous association reaction, and the number of binding sites for juglone on serum albumins was determined to be equal to one.
Abstract: The interaction between juglone at the concentration range of 10–110 µM and bovine serum albumin (BSA) or human serum albumin (HSA) at the constant concentration of 11 µM was investigated by fluorescence and UV absorption spectroscopy under physiological-like condition. Performing the experiments at different temperatures showed that the fluorescence intensity of BSA/HSA was decreased in the presence of juglone by a static quenching mechanism due to the formation of the juglone–protein complex. The binding constant for the interaction was in the order of 103 M−1, and the number of binding sites for juglone on serum albumins was determined to be equal to one. The thermodynamic parameters including enthalpy (ΔH), entropy (ΔS) and Gibb’s free energy (ΔG) changes were obtained by using the van’t Hoff equation. These results indicated that van der Waals force and hydrogen bonding were the main intermolecular forces stabilizing the complex in a spontaneous association reaction. Moreover, the interaction of BSA/HSA with juglone was verified by UV absorption spectra and molecular docking. The results of synchronous fluorescence, UV–visible and CD spectra demonstrated that the binding of juglone with BSA/HSA induces minimum conformational changes in the structure of albumins. The increased binding affinity of juglone to albumin observed in the presence of site markers (digoxin and ibuprofen) excludes IIA and IIIA sites as the binding site of juglone. This is partially in agreement with the results of molecular docking studies which suggests sub-domain IA of albumin as the binding site.
TL;DR: An easy and rapid detection method for assessment of serum exosomal CEA is optimized combining a treatment by volume-excluding polymers to isolate the exosomes, their subsequent solubilization in an assay buffer and ELISA.
Abstract: Background
Serum exosomal proteins have great potential as indicators of disease status in cancer, inflammatory or metabolic diseases. The association of a fraction of various serum proteins such as carcinoembryonic antigen (CEA) with circulating exosomes has been debated. The establishment of a method to measure the exosomal fraction of such proteins might help resolve this controversy. The use of enzyme-linked immunosorbent assays (ELISAs) to measure serum exosomal molecules, for example CEA, is rare in research laboratories and totally absent in clinical biology. In this study, we optimized a method for assessment of serum exosomal molecules combining a treatment by volume-excluding polymers to isolate the exosomes, their subsequent solubilization in an assay buffer and ELISA.
Methods
One hundred sixteen consecutive patients with colorectal cancer were enrolled for this study between June 2015 and June 2016 at Wakayama Medical University Hospital (WMUH). Whole blood samples were collected from patients during surgery. Exosomes were isolated using the ExoQuick reagent, solubilized in an assay buffer and subjected to CEA detection by ELISA. The procedure of serum exosome isolation and the formulation of the assay buffer used for the ELISA were optimized in order to improve the sensitivity and specificity of the assay.
Results
A five-fold increase in the concentration of the exosomes in the assay buffer (using initial serum volume as a reference) and the addition of bovine serum albumin (BSA) resulted in more accurate measurements of the serum exosomal CEA. The thawing temperature of frozen serum samples before exosome extraction was also optimized. A validation study that included one hundred sixteen patients with colorectal cancer demonstrated that serum exosomal CEA from samples thawed at 25°C exhibited a better AUC value, sensitivity, and specificity as well as a more correct classification than serum CEA.
Conclusions
We optimized an easy and rapid detection method for assessment of serum exosomal CEA. The thawing temperature of frozen serum prior to exosome extraction, the formulation of the assay buffer used for exosome solubilization and the concentration of the exosomes in this buffer were fine-tuned to enable the appropriate and accurate measurement of serum exosomal CEA.
TL;DR: Lophirone B seems to be exposed to the aqueous media as well as accommodated inside the protein cavity, resulting in a moderate affinity for the albumin.
TL;DR: Evidence is provided that albumin nanoparticles are suitable carriers of Api and the use of traditional or novel excipients should be taken into consideration.
Abstract: Background: Respiratory diseases are mainly derived from acute and chronic inflammation of the alveoli and bronchi. The pathophysiological mechanisms of pulmonary inflammation mainly arise from oxidative damage that could ultimately lead to acute lung injury. Apigenin (Api) is a natural polyphenol with prominent antioxidant and anti-inflammatory properties in the lung. Inhalable formulations that consist of nanoparticles (NPs) have several advantages over other administration routes, and therefore, this study investigated the application of apigenin-loaded bovine serum albumin nanoparticles (BSA-Api-NPs) for pulmonary delivery. Methods: Dry powder formulations of BSA-Api-NPs were prepared by spray drying and characterized by laser diffraction particle sizing, scanning electron microscopy, differential scanning calorimetry, and powder X-ray diffraction. The influence of dispersibility enhancers (lactose monohydrate and l-leucine) on the in vitro aerosol deposition using a next-generation impactor ...
TL;DR: The present study revealed that poly(ω-methoxyalkyl acrylate)s are useful for blood-contacting medical devices, and PMC3A is the best mode of PMCxA to apply as an antiprotein adsorption coating agent.
TL;DR: Interaction between bovine serum albumin and phosphorus heterocycles (PHs) was studied using multi-spectroscopic techniques and results indicated the high binding affinity of PHs to BSA as it quenches the intrinsic fluorescence of BSA.
TL;DR: In this paper, a quantitative understanding of the interaction between titanium dioxide (TiO2) nanoparticle (22 nm average diameter) and bovine serum albumin (BSA) was carried out to explore the effect of pH on surface coverage and adsorbed protein structure.
Abstract: Protein adsorption on nanoparticle surfaces plays a critical role in biological systems, and bovine serum albumin (BSA) is a useful model protein to study due to its high abundance and similar properties as its human variant. Herein, a quantitative understanding of the interaction between titanium dioxide (TiO2) nanoparticle (22 nm average diameter) and BSA was carried out to explore the effect of pH on surface coverage and adsorbed protein structure. Experiments were conducted under different pH conditions (pH 7.4, 4.5, and 2.0) that simulate the pH of blood, lung, and stomach fluids, respectively. Attenuated total reflectance–Fourier transform infrared (ATR-FTIR) spectroscopy was used for in situ adsorption characterization and protein secondary structure analysis. In addition, thermogravimetric analysis (TGA) was used to provide quantitative determination of the surface coverage. These results show that BSA adsorption on TiO2 highly depends on pH as well as the presence of salts. Furthermore, it is als...
TL;DR: It can be inferred that hydrophobic and electrostatic interactions are the major binding forces involved in formation of the CRB-BSA complex.
TL;DR: The mechanism of SA interaction with bovine serum albumin (BSA) has been investigated by multi-spectroscopic and molecular modeling methods under physiological conditions and indicated that hydrophobic binding plays a main role in the binding of SA to Albumin.