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Updated: Aug 13, 2026
Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
The extraordinary ligand binding properties of human serum albumin
Mauro Fasano1, Stephen Curry, Enzo Terreno
1Department of Structural and Functional Biology, University of Insubria, Center of Neurosciences, 21052 Busto Arsizio, Italy.
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.
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