Topic
Bovine serum albumin
About: Bovine serum albumin is a research topic. Over the lifetime, 19981 publications have been published within this topic receiving 571291 citations. The topic is also known as: BSA.
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TL;DR: The structural changes in horse cytochrome c, bovine ribonuclease A (RNase A), sperm whale myoglobin, ovalbumin, human hemoglobin, and bovines serum albumin during adsorption on ultrafine silica particles have been studied.
213 citations
TL;DR: It is found that the fluorescence of BSA at λ(ex) 230 nm arising from aromatic amino acids Trp and Tyr is almost as sensitive as that achieved at η 280 nm for elucidating the protein conformational changes, which provides a valid and new probe for the investigation of binding kinetics between molecules/ions and proteins.
Abstract: The interactions of imidazolium ionic liquids (ILs), i.e., dibutylimidazolium chloride, 1-butyl-3-methylimidazolium chloride, and 1-butyl-3-methylimidazolium nitrate, with bovine serum albumin (BSA) were studied by monitoring the spectral behaviors of IL-BSA aqueous systems. The intrinsic fluorescence of BSA at 340 nm excited at 230 nm is obviously quenched by these ILs due to complex dynamic collision and their quenching constants are at the order of 10(2) L mol(-1). However, no fluorescence quenching is observed within the same region when excited at 280 nm, which is widely used for probing protein conformations. Thermodynamic investigations reveal that the combination between ILs and BSA is entropy driven by predominantly hydrophobic and electrostatic interactions, leading to the unfolding of polypeptides within BSA. The influence of the ILs on the conformation of BSA follows a sequence of BmimNO(3) > BmimCl ≈ BbimCl. Molecular docking shows that cationic imidazolium moieties of ILs enter the subdomains of protein and interact with the hydrophobic residues of domain III. An agreement between fluorescence spectroscopic investigations and molecular docking is reached. It is found that the fluorescence of BSA at λ(ex) 230 nm arising from aromatic amino acids Trp and Tyr is almost as sensitive as that achieved at λ(ex) 280 nm for elucidating the protein conformational changes, which provides a valid and new probe for the investigation of binding kinetics between molecules/ions and proteins.
213 citations
TL;DR: Dendrimer binding altered BSA conformation with a major reduction of alpha-helix and an increase in random coil and turn structures, indicating a partial protein unfolding.
213 citations
TL;DR: A protein of high molecular weight (approximately 450,000) that is labile at 42 degrees C is described, which among the extremely heat-labile factors is remarkably stabilized by ATP.
Abstract: The ATP-dependent proteolytic cell-free system from reticulocytes has been resolved into three components, each of which is absolutely required for acid solubilization of 125I-labeled bovine serum albumin radioactivity. In addition to the previously reported heat-stable polypeptide [Ciechanover, A., Hod, Y. & Hershko, A. (1978) Biochem. Biophys. Res Commun. 81, 1100-1105], we now describe a protein of high molecular weight (approximately 450,000) that is labile at 42 degrees C. The extremely heat-labile factors is remarkably stabilized by ATP. GTP and CTP, which do not stimulate protolysis, do not stabilize this factor. Adenylate nucleotides such as ADP or the nonhydrolyzable beta,gamma imido or methylene analogues of ATP cause stabilization although they do not activate proteolysis. A third protein component of the protease system, stable at 42 degrees C, has been separated from the heat-labile species by salt precipitation. All three components are required with ATP for proteolytic activity, but thus far only the heat-labile factor has been shown to interact directly with ATP.
212 citations
TL;DR: The conjugates showed an order of magnitude increase in antioxidant activity compared to free drug and when combined with intrinsic and ligand-based targeting with dendrimers, these types of GSH sensitive nanodevices can lead to improved drug release profiles and in vivo efficacy.
212 citations