α-Tocopherol binding to human serum albumin

Gabriella Fanali, Mauro Fasano, Paolo Ascenzi, Jean Marc Zingg, Angelo Azzi

Research output: Contribution to journalArticlepeer-review

Abstract

Given the ability of human serum albumin (HSA) to bind hydrophobic ligands, the binding mode of α-tocopherol, the most representative member of the vitamin E family, is reported. α-Tocopherol binds to HSA with K $_{\rm d}^0$ = (7.0 ± 3.0) × 10-6 M (pH 7.2, 25.0°C). Competitive and allosteric modulation of α-tocopherol binding to full-length and truncated (Asp1-Glu382) HSA by endogenous and exogenous ligands suggests that it accommodates preferentially in the FA3-FA4 site. As HSA is taken up into cells, colocalizes with the α-tocopherol transfer protein, and contributes to ligand secretion via ABCA1, it might participate in the distribution of α-tocopherol between plasma, cells, and tissues.

Original languageEnglish
Pages (from-to)294-303
Number of pages10
JournalBioFactors
Volume39
Issue number3
DOIs
Publication statusPublished - May 2013

Keywords

  • α-tocopherol
  • Binding mode
  • FA3-FA4 cleft
  • Human serum albumin
  • Thermodynamics

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Molecular Medicine

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