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.
de Kroon
A I
AI
Centre for Biomembranes and Lipid Enzymology, University of Utrecht, The Netherlands.
de Gier
J
J
de Kruijff
B
B
D066298:In Vitro Techniques; D008563:Membrane Lipids; D008564:Membrane Potentials; D008565:Membrane Proteins; D009842:Oligopeptides / Q000138:chemical synthesis; D010713:Phosphatidylcholines; D011188:Potassium / Q000502:physiology
D008563:Membrane Lipids; D008565:Membrane Proteins; D009842:Oligopeptides; D010713:Phosphatidylcholines; D011188:Potassium