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α-Tocopherol binding to human serum albumin

Authors

  • Gabriella Fanali,

    Corresponding author
    1. Division of Biomedical Sciences, Department of Theoretical and Applied Sciences, Center of Neuroscience, University of Insubria, Busto Arsizio (VA), Italy
    • Department of Theoretical and Applied Sciences, University of Insubria, Via Alberto da Giussano 12, I-21052 Busto Arsizio, Italy
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    • Tel.: +39 0331 339414; Fax: +39 0331 339459

  • Mauro Fasano,

    1. Division of Biomedical Sciences, Department of Theoretical and Applied Sciences, Center of Neuroscience, University of Insubria, Busto Arsizio (VA), Italy
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  • Paolo Ascenzi,

    1. Interdepartmental Laboratory for Electron Microscopy, University Roma Tre, Roma, Italy
    2. National Institute of Biostructures and Biosystems, Roma, Italy
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  • Jean-Marc Zingg,

    1. Vascular Biology Laboratory, Jean Mayer USDA Human Nutrition Research Center on Aging, Tufts University, Boston, MA, USA
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  • Angelo Azzi

    1. Vascular Biology Laboratory, Jean Mayer USDA Human Nutrition Research Center on Aging, Tufts University, Boston, MA, USA
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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 equation image = (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

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