The motional properties of the hydrophobic fluorescent probe 1,6-diphenyl-1,3,5-hexatriene have been assessed in liposomes of various lecithins: dipalmitoylphosphatidylcholine (DPPC), dioleoylphosphatidylcholine, 1-palmitoyl-2-oleoylphosphatidylcholine (POPC), 1-palmitoyl-2-linoleoylphosphatidylcholine (PLPC), and 1-palmitoyl-2-arachidonoylphosphatidylcholine (PAPC). The temperature dependence of the steady-state fluorescence anisotropy was determined within the range of 10-50°C. Nanosecond measurements were also made and the results analyzed by a model of wobbling diffusion confined within a cone. In this treatment the cone angle (θc) obtained relates to the degree of order of the fatty acyl chains, and the wobbling diffusion constant (Dw) relates to the rate of motion of the hydrocarbon chains. θc was increased (order decreased) and Dw increased (rate increased) for the first double bond (POPC) as compared to the fully saturated DPPC. In all four unsaturated lecithins the temperature dependences of θc and Dw were similar: θc increased by about 4-5°, and Dw increased by a factor of 1.5 per 10°C. DPPC in the liquid-crystalline phase also showed a similar trend. The absolute values, on the other hand, showed some differences: for θc, DOPC (78° at 37°C) > PAPC (75°) > POPC (70°) ≃ PLPC (69°) > DPPC (20°), and for Dw, PAPC (0.28 ns-1) > DOPC (0.22 ns-1) ≃ PLPC (0.24 ns-1) > POPC (0.21 ns-1) > DPPC (0.05 n-1). The differences among the unsaturated lecithins are relatively small suggesting that the first double bond introduced into a lecithin plays the most important role at physiological temperatures. In 1:1 mixtures of the disaturated lecithin, DPPC, with the unsaturated lecithins, the temperature of the phase transition of the former was lowered and broadened, by approximately the same amount, irrespective of the differences in unsaturation.
|Number of pages||6|
|Publication status||Published - 1981|
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