Topic
Human serum albumin
About: Human serum albumin is a research topic. Over the lifetime, 9402 publications have been published within this topic receiving 269029 citations. The topic is also known as: serum albumin & ALB.
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TL;DR: The binding of the fluorescent probe acrylodan to human serum albumin was studied by fluorescence spectroscopy and it was suggested that AC should also bind the human albumin in the primary site of bilirubin, but with less affinity than to the cysteine‐34.
Abstract: The binding of the fluorescent probe acrylodan (AC) to human serum albumin (HSA) was studied by fluorescence spectroscopy. The binding isotherms could be fitted to two types of sites. Competition experiments using io-doacetamide suggested that AC binds tightly on HSA by the cysteine-34. Attempts were made to find the location of the second site using high concentrations of warfarin, phenylbutazone, diazepam, indomethacin, palmitic acid or bilirubin in order to displace the bound AC to the HSA. Bilirubin was the only ligand able to displace the bound AC. This result suggests that AC, which is a very hydrophobic molecule also capable of labeling lysine residues, should also bind the human albumin in the primary site of bilirubin, but with less affinity than to the cysteine-34.
73 citations
TL;DR: The results indicate that an automated "ligand-fishing" technique can be developed using magnetic beads containing an immobilized protein to isolate known HSA ligands from a mixture containing ligands and nonligands.
Abstract: Human serum albumin, HSA, was immobilized onto the surface of silica-based magnetic beads. The beads were used to isolate known HSA ligands from a mixture containing ligands and nonligands. The separation was accomplished manually and was also automated. The results indicate that an automated "ligand-fishing" technique can be developed using magnetic beads containing an immobilized protein.
73 citations
TL;DR: This present investigation has revealed that steady state as well as time-resolved fluorescence techniques can serve as highly sensitive monitors for exploring the interaction of fluorescent probe 1-anthracene sulphonate with model transport proteins, bovine serum albumin (BSA) and human serumalbumin (HSA).
73 citations
TL;DR: The results demonstrate that the blood protein components contribute to the inflammatory effects of nanosheets and provide important insights for the nanosafety evaluation and the rational design of nanomedicines in the future.
Abstract: Two-dimensional (2D) nanosheets (NSs) have a large surface area, high surface free energy, and ultrathin structure, which enable them to more easily penetrate biological membranes and promote adsorption of drugs and proteins. NSs are capable of adsorbing a large amount of blood proteins to form NSs-protein corona complexes; however, their inflammatory effects are still unknown. Therefore, we investigated the pro-inflammatory effect of 2D model nanosheet structures, molybdenum disulfide (MoS2), and the MoS2 NSs-protein complexes with four abundant proteins in human blood, i.e., human serum albumin (HSA), transferrin (Tf), fibrinogen (Fg), and immunoglobulin G (IgG). The interactions between the NSs and the proteins were analyzed by quantifying protein adsorption, determining binding affinity, and correlating structural changes in the protein corona with the uptake of NSs by macrophages and the subsequent inflammatory response. Although all of the NSs-protein complexes induced inflammation, IgG-coated and Fg-coated NSs triggered much stronger inflammatory effects by producing and releasing more cytokines. Among the four proteins, IgG possessed the highest proportion of β-sheets and led to fewer secondary structure changes on the MoS2 nanosheets. This can facilitate uptake and produce a stronger pro-inflammatory response in macrophages due to the recognition of an NSs-IgG complex by Fc gamma receptors and the subsequent activation of the NF-κB pathways. Our results demonstrate that the blood protein components contribute to the inflammatory effects of nanosheets and provide important insights for the nanosafety evaluation and the rational design of nanomedicines in the future.
73 citations
TL;DR: The accommodation of ZnPP into the protein matrix efficiently eliminated the collisional triplet self-quenching process and the addition of a water-soluble electron acceptor, MV2+, resulted in a significant decrease in the triplet lifetime.
Abstract: We present the photophysical properties of complexes of recombinant human serum albumin (rHSA) with Zn(II)−protoporphyrin IX (ZnPP) and their activities in the photosensitized reduction of water to hydrogen (H2) using methyl viologen (MV2+) as an electron relay. The ZnPP is bound in subdomain IB of wild-type rHSA [rHSA(wt)] by an axial coordination of Tyr-161 and, in the rHSA(I142H/Y161L) mutant [rHSA(His)], by a His-142 coordination. Both the rHSA(wt)−ZnPP and rHSA(His)−ZnPP complexes showed a long-lived photoexcited triplet state with lifetimes (τT) of 11 and 2.5 ms, respectively. The accommodation of ZnPP into the protein matrix efficiently eliminated the collisional triplet self-quenching process. The addition of a water-soluble electron acceptor, MV2+, resulted in a significant decrease in the triplet lifetime. The transition absorption spectrum revealed the oxidative quenching of rHSA−3ZnPP* by MV2+. The quenching rate constant (kq) and backward electron transfer rate constant (kb) were determined t...
73 citations