title: Association of synthetic model peptides with phospholipid vesicles induced by a membrane potential.
abstract: 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.
authors.affiliation: Centre for Biomembranes and Lipid Enzymology, University of Utrecht, The Netherlands.
authors.forename: A I
authors.initials: AI
authors.lastname: de Kroon
authors.forename: J
authors.initials: J
authors.lastname: de Gier
authors.forename: B
authors.initials: B
authors.lastname: de Kruijff
mesh_terms: D066298:In Vitro Techniques; D008563:Membrane Lipids; D008564:Membrane Potentials; D008565:Membrane Proteins; D009842:Oligopeptides / Q000138:chemical synthesis; D010713:Phosphatidylcholines; D011188:Potassium / Q000502:physiology
chemical_list: D008563:Membrane Lipids; D008565:Membrane Proteins; D009842:Oligopeptides; D010713:Phosphatidylcholines; D011188:Potassium