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Updated: Aug 19, 2026

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves
Published on: March 9, 2014
Fluorescent tocopherols as probes of inter-vesicular transfer catalyzed by the alpha-tocopherol transfer protein
Jeffrey K Atkinson1, Phillip Nava, Grant Frahm
1Department of Chemistry and Centre for Biotechnology, Brock University, St. Catharines, Ontario, Canada. jatkin@brocku.ca
Abstract:
Novel fluorescent analogues of alpha-tocopherol have been prepared that incorporate the useful fluorophores nitrobenoxadiazyl (NBD) and anthroyloxy (AO). Both fluorescent tocopherol analogues bind specifically to recombinant human tocopherol transfer protein (hTTP). The NBD-alpha-tocopherol is particularly useful for protein-binding assays, whereas the AO-alpha-tocopherol was designed to be one of a pair of chromophores for a fluorescence resonance energy transfer (FRET) assay of intervesicular tocopherol transfer. It is now possible to follow AO-alpha-tocopherol transfer from donor lipid vesicles composed of predominantly phosphatidylcholine (PC) to acceptor lipid vesicles containing PC and a quenching lipid NBD-PE (2-dipalmitoyl-sn-glycero-3-phosphoethanolamine-N-[7-nitro-2-1,3-benzoxadiazol-4-yl]). The presence of hTTP substantially increases the rate of AO-alpha-tocopherol transfer over the uncatalyzed spontaneous rate.
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