The extraordinary ligand binding properties of human serum albumin

Mauro Fasano, Stephen Curry, Enzo Terreno, Monica Galliano, Gabriella Fanali, Pasquale Narciso, Stefania Notari, Paolo Ascenzi

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)787-796
Number of pages10
JournalIUBMB Life
Volume57
Issue number12
DOIs
Publication statusPublished - Dec 2005

Keywords

  • Allostery
  • Human serum albumin
  • Ligand binding properties
  • Structural aspects

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Fasano, M., Curry, S., Terreno, E., Galliano, M., Fanali, G., Narciso, P., Notari, S., & Ascenzi, P. (2005). The extraordinary ligand binding properties of human serum albumin. IUBMB Life, 57(12), 787-796. https://doi.org/10.1080/15216540500404093