title: The extraordinary ligand binding properties of human serum albumin.
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.
authors.affiliation: Department of Structural and Functional Biology, University of Insubria, Center of Neurosciences, 21052 Busto Arsizio, Italy.
authors.forename: Mauro
authors.initials: M
authors.lastname: Fasano
authors.forename: Stephen
authors.initials: S
authors.lastname: Curry
authors.forename: Enzo
authors.initials: E
authors.lastname: Terreno
authors.forename: Monica
authors.initials: M
authors.lastname: Galliano
authors.forename: Gabriella
authors.initials: G
authors.lastname: Fanali
authors.forename: Pasquale
authors.initials: P
authors.lastname: Narciso
authors.forename: Stefania
authors.initials: S
authors.lastname: Notari
authors.forename: Paolo
authors.initials: P
authors.lastname: Ascenzi
mesh_terms: D000494:Allosteric Regulation; D003287:Contrast Media / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D004364:Pharmaceutical Preparations / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D003287:Contrast Media; D008024:Ligands; D004364:Pharmaceutical Preparations; D012709:Serum Albumin