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.

Fasano, M., Curry, S., Terreno, E., Galliano, M., Fanali, G., Narciso, P., et al. (2005). The extraordinary ligand binding properties of human serum albumin. IUBMB LIFE, 57, 787-796 [10.1080/15216540500404093].

The extraordinary ligand binding properties of human serum albumin

ASCENZI, Paolo
2005-01-01

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.
Fasano, M., Curry, S., Terreno, E., Galliano, M., Fanali, G., Narciso, P., et al. (2005). The extraordinary ligand binding properties of human serum albumin. IUBMB LIFE, 57, 787-796 [10.1080/15216540500404093].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11590/159064
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