Format

Send to

Choose Destination
IUBMB Life. 2005 Dec;57(12):787-96.

The extraordinary ligand binding properties of human serum albumin.

Author information

1
Department 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.

PMID:
16393781
DOI:
10.1080/15216540500404093
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center