The fusion peptide of simian immunodeficiency virus and the phase behaviour of N-methylated dioleoylphosphatidylethanolamine.

Temperature-scan X-ray scattering was used to study the effect of the fusion peptide of simian immunodeficiency virus (SIV) on the lipid polymorphism of N-methylated dioleoylphosphatidylethanolamine (DOPE-Me), in the presence and absence of one or both of the fusion inhibitors carbobenzoxy-D-phenylalanine-L-phenylalanine-glycine and 1-lauroyl-2-hydroxy-sn-glycero-3-phosphocholine (LPC). Using X-ray diffraction at stations 2.1 and 8.2 of the Synchrotron Radiation Source at Daresbury Laboratory, UK, the structure of multilamellar vesicles (MLVs) was probed as the temperature was raised from 20 to 90 degrees C. The results are compared to those of similar studies, reported earlier, that used the fusion peptide of feline leukaemia virus (FeLV) which, at 28 amino acid residues in length, is considerably longer than the SIV peptide (12 amino acid residues). We interpret the results within the framework of current understanding of membrane fusion, and demonstrate how observed lipid polymorphism might describe the fusion process.