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α-Tocopherol binding to human serum albumin.


Biofactors. 2013 Jan 28;


Authors: Fanali G, Fasano M, Ascenzi P, Zingg JM, Azzi A


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. © 2013 BioFactors, 2013.

PMID: 23355326 [PubMed - as supplied by publisher]