Abstract
The most prominent features responsible for binding of flavonoid aglycones to the IIA region of human serum albumin (HSA) were determined based onin vitrofluorescence measurements and density functional theory calculations.
Highlights
IntroductionHuman serum albumin (HSA) is the most abundant protein in human plasma (60%, w/w),[1] which structure has been determined crystallographically
Human serum albumin (HSA) is the most abundant protein in human plasma (60%, w/w),[1] which structure has been determined crystallographically. It is a 585-residue monomeric protein comprised of three homologous domains (I–III), each of which is composed of two subdomains (A and B) (Fig. 1).[2]
density functional theory (DFT) calculations for structure–affinity relationship of avonoid binding to HSA
Summary
Human serum albumin (HSA) is the most abundant protein in human plasma (60%, w/w),[1] which structure has been determined crystallographically It is a 585-residue monomeric protein comprised of three homologous domains (I–III), each of which is composed of two subdomains (A and B) (Fig. 1).[2] These domains play a central role in binding of various endo- and exogenous compounds, hydrophobic organic anions of medium size (100 to 600 Da), e.g. bilirubin, long-chain fatty acids, hematin, thyroxin.[3] Many drugs bind to one of the two primary binding sites, located in subdomains IIA and IIIA (Sudlow sites I and II, respectively), with IIA being the most prominent one.[4,5] The IIA subdomain appears to be spacious and is comprised of several individual binding sites which can accommodate ligands characterized by very different chemical structures. The IIIA site is smaller and less exible and can accommodate only structurally similar ligands.[6]
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