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The extraordinary ligand binding properties of human serum albumin
Author(s) -
Fasano Mauro,
Curry Stephen,
Terreno Enzo,
Galliano Monica,
Fanali Gabriella,
Narciso Pasquale,
Notari Stefania,
Ascenzi Paolo
Publication year - 2005
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540500404093
Subject(s) - human serum albumin , chemistry , allosteric regulation , ligand (biochemistry) , plasma protein binding , serum albumin , albumin , binding site , biochemistry , receptor
Human serum albumin (HSA), the most prominent protein in plasma, binds different classes of ligands at multiple sites. HSA provides a depot for many compounds, affects pharmacokinetics of many drugs, holds some ligands in a strained orientation providing their metabolic modification, renders potential toxins harmless transporting them to disposal sites, accounts for most of the antioxidant capacity of human serum, and acts as a NO‐carrier. The globular domain structural organization of monomeric HSA is at the root of its allosteric properties which are reminiscent of those of multimeric proteins. Here, structural, functional, biotechnological, and biomedical aspects of ligand binding to HSA are summarized.