The extraordinary ligand binding properties of human serum albumin
Mauro Fasano(University of Insubria), Stephen Curry(Imperial College London), Enzo Terreno(University of Turin), Monica Galliano(University of Pavia), Gabriella Fanali(University of Insubria), Pasquale Narciso(Istituto Nazionale per le Malattie Infettive Lazzaro Spallanzani), Stefania Notari(Istituto Nazionale per le Malattie Infettive Lazzaro Spallanzani), Paolo Ascenzi(Istituto Nazionale per le Malattie Infettive Lazzaro Spallanzani)
Cited by 1,069Open Access
Abstract
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.