Revisiting Peptide Amphiphilicity for Membrane Pore Formation

• DOI: 10.1021/bi201335t
• Publication Date: 2011-09-26T15:22:36Z
• Authors: Aurélien Lorin; Mathieu Noël; Marie-Ève Provencher; Vanessa Turcotte; Carole Masson; Sébastien Cardinal; Patrick Lagüe; Normand Voyer; Michèle Auger
• Keywords: Calcein

It has previously been shown that an amphipathic de novo designed peptide made of 10 leucines and four phenylalanines substituted with crown ethers induces vesicle leakage without selectivity. To gain selectivity against negatively charged dimyristoylphosphatidylglycerol (DMPG) bilayers, one or two the were positively residues at each position. All peptides induce significant calcein DMPG vesicles. However, some do not zwitterionic dimyristoylphosphatidylcholine vesicles are thus active only bacterial model membranes. The intravesicular is induced by pore formation instead membrane micellization. Nonselective mostly helical, while selective mainly adopt intermolecular β-sheet structure. This study therefore demonstrates position lysine significantly influences secondary structure bilayer 14-mer peptide, being more than helical peptides.