title: Fluorescence studies of dipalmitoylphosphatidylcholine vesicles reconstituted with the glycoprotein of vesicular stomatitis virus.
abstract: The vesicular stomatitis virus glycoprotein (G) was reconstituted into dipalmitoylphosphatidylcholine (DPPC) vesicles by detergent dialysis. The DPPC gel to liquid-crystalline phase transition of the DPPC-G protein vesicles was monitored by the fluorescence anisotrophy of trans-paranaric acid, 16-(9-anthroyloxy)palmitoylglucocerebroside, 1,6-diphenyl-1,3,5-hexatriene, and 4-heptadecyl-7-hydroxycoumarin. The DPPC transition temperature measured by all four fluorescent probes was lowered in the presence of the G protein and the DPPC gel state was disordered by the G protein as evidenced by a decreased fluorescence anisotropy for all four probes below the phase-transition temperature. A possible ordering of the DPPC liquid-crystalline state by the G protein was indicated by an increased anisotropy of trans-paranaric acid and 16-(9-anthroyloxy)palmitoylglucocerebroside in the liquid-crystalline state of DPPC-G protein vesicles. The G protein in addition affected the ionization of the 4-heptadecyl-7-hydroxycoumarin in lipid vesicles, increasing the apparent pK of the probe from 9.05 to 9.45.
mesh_terms: D004161:Diphenylhexatriene; D005231:Fatty Acids, Unsaturated; D005454:Fluorescence Polarization; D005456:Fluorescent Dyes; D006023:Glycoproteins / Q000302:isolation & purification; D007700:Kinetics; D011663:Pulmonary Surfactants; D014721:Vesicular stomatitis Indiana virus; D014764:Viral Proteins / Q000302:isolation & purification
chemical_list: D005231:Fatty Acids, Unsaturated; D005456:Fluorescent Dyes; D006023:Glycoproteins; D011663:Pulmonary Surfactants; D014764:Viral Proteins; D004161:Diphenylhexatriene; C013641:parinaric acid