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: In healthy elderly subjects, f(HMA) was significantly lower than in healthy young male subjects, indicating that HSA in the elderly becomes more oxidized than in the young subjects, suggesting that one of the important functions of serum albumin could be to participate in the maintenance of a constant redox potential in the extracellular fluids, thus securing a certain redox buffer capacity.
108 citations
TL;DR: Human serum albumin is acetylated when exposed to acetylsalicylic acid (aspirin) under physiologic conditions in vitro and indications are that a similar phenomenon occurs in vivo after ingestion of aspirin.
Abstract: Human serum albumin is acetylated when exposed to acetylsalicylic acid (aspirin) under physiologic conditions in vitro. Indications are that a similar phenomenon occurs in vivo after ingestion of aspirin.
108 citations
TL;DR: The zeta potential results suggested that both hydrophobic and electrostatic interactions played important roles in the protein–metformin complex formation.
Abstract: The interaction between metformin and human serum albumin (HSA), as well as its glycated form (gHSA) was investigated by multiple spectroscopic techniques, zeta potential, and molecular modeling under physiological conditions. The steady state and time-resolved fluorescence data displayed the quenching mechanism of HSA-metformin and gHSA-metformin was static. The binding information, including the binding constants, number of binding sites, effective quenching constant showed that the binding affinity of metformin to HSA was greater than to gHSA which also confirmed by anisotropy measurements. It was determined that metformin had two and one set of binding sites on HSA and gHSA, respectively. Far-UV CD spectra of proteins demonstrated that the α-helical content decreased with increasing metformin concentration. The zeta potential and resonance light scattering (RLS) diagrams provided that lower drug concentration induced metformin aggregation on gHSA surface as compare to HSA. The increase in polarizability was one of the important factors for the enhancement of RLS and the formation of drug/protein complexes. The zeta potential results suggested that both hydrophobic and electrostatic interactions played important roles in the protein-metformin complex formation. Site marker experiments and molecular modeling showed that the metformin bound to subdomain IIIA (Sudlow's site II) on HSA and gHSA.
108 citations
TL;DR: Structural changes associated with the exposure of human serum albumin to glucose with or without the presence of Cu (II) have been characterized using a bank of methods for structural analysis including circular dichroism, amino acid analysis, fluorescence measurements, SDS-PAGE, and boronate binding.
108 citations
TL;DR: In this paper, the interaction of rofecoxib with human serum albumin (HSA) under physiological condition was investigated by fluorescence, UV-vis absorbance and Fourier transfer infrared (FT-IR) spectroscopy.
Abstract: The interaction of rofecoxib with human serum albumin (HSA) under physiological condition was investigated by fluorescence, UV–vis absorbance and Fourier transfer infrared (FT-IR) spectroscopy. Fluorescence data revealed that the fluorescence quenching of HSA by rofecoxib was the result of the formed complex of HSA–rofecoxib, and the site binding constants ( K a ) were 4.840 × 10 4 , 3.450 × 10 4 , and 2.325 × 10 4 M −1 at 298, 304, and 310 K, respectively. The thermodynamic parameters, enthalpy change (Δ H ) and entropy change (Δ S ) for the reaction were calculated to be −46.90 kJ mol −1 and −67.59 J mol −1 K −1 according to van’t Hoff equation. The spectroscopic measurements and the thermodynamic parameters suggested that van der Waals interaction and hydrogen bonds were the predominant intermolecular forces to stabilize the complex. The distance r = 5.1 nm between donor (Trp 214 ) and accepter (rofecoxib) was obtained according to the Forster theory of non-radiative energy transfer. FT-IR spectra and UV–vis absorbance showed that the change of protein secondary structures resulted from the rofecoxib binding to several amino acids on the hydrophobic pocket of HSA. Furthermore, it is observed from the probe of competitive experiments that the binding location of rofecoxib with HSA could be the same as the warfarin site I of HSA, which was also revealed by fluorescence anisotropy.
108 citations