Association of synthetic model peptides with phospholipid vesicles induced by a membrane potential.

Hydrophobic model peptides, consisting of 5 or 6 amino acids and carrying a net positive charge at the amino terminus, exhibit a dramatically increased association with large unilamellar egg-PC vesicles upon application of a valinomycin-induced K+ diffusion potential, negative inside. The association of the peptides is largely reversible, apparent from a release of peptide upon dissipation of the membrane potential.