H-aggregation of azobenzene-substituted amphiphiles in vesicular membranes.

Photochemical switching has been studied of double-tailed phosphate amphiphiles containing azobenzene units in both tails in aqueous vesicular dispersions and in mixed vesicular systems with 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC). Since the ease of switching depends on the strength of the bilayer packing, particular emphasis has been placed on the occurrence of H-aggregation in the hydrophobic core of the vesicles. UV-vis spectrometry was employed to monitor H-aggregation and showed how this process depends on the ionic strength and on the mode of preparation of the vesicles. Two types of H-aggregates were observed in mixed DOPC vesicles with 5 mol % of azobenzene phosphate: one with lambda(max) at around 300 nm and one with lambda(max) at 305-320 nm. Those with lambda(max) at 300 nm could not be trans-cis photoisomerized, whereas those with lambda(max) at 305-320 nm are more loosely packed and can be photochemically switched. The permeability of the vesicular bilayers, as probed with leakage experiments using calcein as a fluorescent probe, was examined as another measure for the strength of bilayer packing. Leakage occurred only for DOPC vesicles containing more than 20 mol % of azobenzenephosphate, irradiated with UV light to induce trans-cis photoisomerization. We contend that detailed information on bilayer packing will be of crucial importance for fine-tuning the lateral pressure in vesicular membranes with the ultimate aim to steer the opening and closing of mechanosensitive protein channels of large conductance.