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Effect of Bilayer Phospholipid Composition and Curvature on Ligand Transfer by the α‐Tocopherol Transfer Protein
Author(s) -
Zhang Wen Xiao,
Frahm Grant,
Morley Samantha,
Manor Danny,
Atkinson Jeffrey
Publication year - 2009
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/s11745-009-3310-x
Subject(s) - förster resonance energy transfer , chemistry , ligand (biochemistry) , phospholipid , acceptor , vesicle , fluorescence , lipid bilayer , membrane , membrane curvature , bilayer , biophysics , photochemistry , biochemistry , receptor , physics , quantum mechanics , biology , condensed matter physics
We report here our preliminary investigations on the mechanism of α‐TTP‐mediated ligand transfer as assessed using fluorescence resonance energy transfer (FRET) assays. These assays monitor the movement of the model α‐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 α‐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 α‐TTP dominating the binding energy between protein and membrane.