Influence of the gel-liquid phase transition on hematoporphyrin triplet deactivation in liposomes.

The deactivation of the triplet state of hematoporphyrin and its dimethyl ester in unilamellar liposomes of dipalmitoyl phosphatidylcholine was studied by nanosecond laser flash photolysis. It was found that the rate of deactivation increases abruptly on raising the temperature in the region of the gel-liquid phase transition of the lipid bilayer (41 degrees C). The rate of change has its maximum at 38.4 +/- 0.5 degree C for both porphyrins. This variation is due to the high lateral mobility of the porphyrins in the liquid-crystal bilayer, which enhances the rates of concentration triplet quenching and triplet-triplet annihilation.