Peptide-induced membrane fusion: Towards the understanding of the mechanism of protein-induced fusion

摘要

The fusogenic properties of an amphipathic net-negatively charged peptide (WAE 11), consisting of 11 amino acid residues, were studied. Whereas the free peptide displays no significant fusion activity, it is demonstrated that membrane fusion is strongly promoted when the peptide is anchored to a liposomal membrane. Fusion is optimal at neutral pH, and occurs essentially in a non-leaky fashion. Hydrophobic interactions, involving shallow penetration of the peptide into the target membrane, facilitate the fusion event, as revealed by changes in intrinsic fluorescence, in conjunction with KI-quenching studies. Such a penetration appears to be regulated by lipid head group spacing.