Document Detail


α-Tocopherol binding to human serum albumin.
MedLine Citation:
PMID:  23355326     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Gabriella Fanali; Mauro Fasano; Paolo Ascenzi; Jean-Marc Zingg; Angelo Azzi
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-28
Journal Detail:
Title:  BioFactors (Oxford, England)     Volume:  -     ISSN:  1872-8081     ISO Abbreviation:  Biofactors     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8807441     Medline TA:  Biofactors     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013 International Union of Biochemistry and Molecular Biology, Inc.
Affiliation:
Division of Biomedical Sciences, Department of Theoretical and Applied Sciences, Center of Neuroscience, University of Insubria, Busto Arsizio (VA), Italy. gabriella.fanali@uninsubria.it.
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