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2. Effect of Bilayer Phospholipid Composition and Curvature on Ligand Transfer by the α‐Tocopherol Transfer Protein

Author

Grant Frahm, Jeffrey Atkinson, Samantha Morley, Wen Xiao Zhang, and Danny Manor

Subjects
Membrane Fluidity, Lipid Bilayers, alpha-Tocopherol, Phospholipid, Biological Transport, Active, Ligands, Biochemistry, Article, chemistry.chemical_compound, Humans, Phospholipids, Chemistry, Ligand, Bilayer, Vesicle, Organic Chemistry, Cell Biology, Acceptor, Crystallography, Förster resonance energy transfer, Membrane curvature, Liposomes, Carrier Proteins, Energy Metabolism, Hydrophobic and Hydrophilic Interactions, Plant lipid transfer proteins
Abstract

We report here our preliminary investigations on the mechanism of alpha-TTP-mediated ligand transfer as assessed using fluorescence resonance energy transfer (FRET) assays. These assays monitor the movement of the model alpha-tocopherol fluorescent derivative ((R)-2,5,7,8-tetramethyl-chroman-2-[9-(7-nitro-benzo[1,2,5]oxadiazol-4-yl amino)-nonyl]-chroman-6-ol; NBD-Toc) from protein to acceptor vesicles containing the fluorescence quencher TRITC-PE. We have found that alpha-TTP utilizes a collisional mechanism of ligand transfer requiring direct protein-membrane contact, that rates of ligand transfer are greater to more highly curved lipid vesicles, and that such rates are insensitive to the presence of anionic phospholipids in the acceptor membrane. These results point to hydrophobic features of alpha-TTP dominating the binding energy between protein and membrane.

Published
2009
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