Cationic polypeptide-induced fusion of acidic liposomes.

Fusion of acidic liposomes was induced by Mg2+, Ca2+, polylysine and polymyxin B. The extent of fusion and the concomitant change in liposome permeability induced by divalent cations depended on the concentration of liposomes in the suspension as well as on the cation concentration. In contradistinction, the extent of fusion and the change in permeability induced by the polypeptides depended only on the polycation concentration. The difference in the pattern of interaction, between the liposomes and the various cations, is a result of different binding affinities. The binding of the polypeptides to the liposomes, in contrast to divalent cations, is practically irreversible. The potential of polylysine to induce fusion of acidic phosphatidyl-ethanolamine-devoid liposomes was used to demonstrate that in order to obtain fusion, both membranes involved must be susceptible, at least to a certain degree, to fusion by the proper inducer. When lysophosphatidylcholine substituted for phosphatidylcholine in phosphatidylethanolamine-rich acidic liposomes, extensive polylysine-induced fusion was obtained without concomitant spillage of the liposome contents.