A. Schanck et al., DESTABILIZATION OF A MODEL MEMBRANE BY A PREDICTED FUSION PEPTIDE OF FERTILIN-ALPHA, Journal de chimie physique et de physico-chimie biologique, 95(2), 1998, pp. 467-473
The subunit alpha of the guinea pig fertilin (previously known as PH-3
0, an integral membrane protein involved in sperm-egg binding and fusi
on) is predicted to be a potential fusion protein. The structure of th
is putative fusion protein was analysed by molecular modeling and we h
ave found a peptidic sequence of 17 residues (D-83-P-99) organized in
helix that inserts obliquely in lipid phases. The effect of this synth
esized peptide was studied on a model membrane by P-31 NMR and light s
cattering, It appears to increase the size of lipid vesicles and induc
es structural modifications. We interpret these observations as a dest
abilization of the lipid organization by this peptide because of its t
ilted insertion in phospholipid layers. This destabilization could fav
or membrane fusion.