17 August 1994 Time-resolved fluorescence studies of a transmembrane peptide sequence of the dopamine D2 receptor
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Highly hydrophobic peptides in small unilamellar vesicles can be used to model membrane-embedded proteins such as the dopamine D2 receptor. The transmembrane domains of the dopamine D2 receptor are known to contain residues corresponding to the binding sites for natural receptor ligands. We have developed a model system consisting of a peptide whose sequence was taken from the transmembrane region of the dopamine D2 receptor and incorporated it into phospholipid bilayers. This polypeptide sequence, NH2-D-V-L-Y-S-A-F-T-W-L-G-Y-V-N-S-A-V-N-P-I-I-Y-T- T-F-N-V-CO2H, contains a single tryptophan residue, whose fluorescence properties provides an intrinsic probe of the microenvironment of the peptide within the bilayer. Purification of this highly hydrophobic peptide required the development of a novel alcohol-based reversed-phase HPLC solvent system. The vesicles were produces by cosonication of the peptide with dimyristoylphosphatidylcholine lipid and were characterized by electron microscopy and fluorescence spectroscopy. Time- correlated single photon counting was sued to measure the fluorescence anisotropy of the system as a function of temperature across the lipid phase transition range and as a function of the peptide/lipid ratio.
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Valerie L. Williams, Valerie L. Williams, Scott H. Courtney, Scott H. Courtney, David I. Schuster, David I. Schuster, Randall B. Murphy, Randall B. Murphy, } "Time-resolved fluorescence studies of a transmembrane peptide sequence of the dopamine D2 receptor", Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); doi: 10.1117/12.182759; https://doi.org/10.1117/12.182759

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