[Effect of sterols on melittin incorporation into liposomal membranes]

Effects of various sterols on the values of intensity, spectrum position and polarization of tryptophan fluorescence (P) of melittin incorporated in lecithin liposomes at different lipid/protein molar ratios (Ri) were studied. A difference in sterol effects has been revealed at the values of Ri > 5. At Ri < 5, fluorescence parameters were determined mainly by melittin in the aqueous solution. Assuming that melittin was bound to lecithin, the lecithin/melittin binding ratio was found to be in the range of 25-50. Unlike cholesterol and stigmasterol, the incorporation into membranes of ergosterol and 7-dehydrocholesterol produced a decrease in the intensity of tryptophan fluorescence and an increase in the P value. This difference might result from the presence of an additional double bond in one of sterol rings of ergosterol and 7-dehydrocholesterol molecules. Analysis of the results obtained enabled us to suggest that the structure of the steroid B ring is responsible for the effect exerted by sterols on melittin-lipid interactions.