Fluorescent Tocopherols as Probes of Inter-Vesicular Transfer Catalyzed by the α-Tocopherol Transfer Protein
| Autor: | Phillip Nava, Jeffrey Atkinson, Valerie Curtis, Grant Frahm, Danny Manor |
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| Rok vydání: | 2004 |
| Předmět: |
Tocopherols
General Biochemistry Genetics and Molecular Biology law.invention chemistry.chemical_compound History and Philosophy of Science law Phosphatidylcholine Fluorescence Resonance Energy Transfer Humans heterocyclic compounds Tocopherol Fluorescent Dyes Quenching (fluorescence) General Neuroscience food and beverages Biological Transport Acceptor Fluorescence Förster resonance energy transfer Biochemistry chemistry Liposomes Recombinant DNA Biophysics lipids (amino acids peptides and proteins) Carrier Proteins Plant lipid transfer proteins |
| Zdroj: | Annals of the New York Academy of Sciences. 1031:324-327 |
| ISSN: | 1749-6632 0077-8923 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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