title: Investigation of the mechanism of action of novel amphipathic peptides: insights from solid-state NMR studies of oriented lipid bilayers.
abstract: We have investigated in the present study the effect of both non-selective and selective cationic 14-mer peptides on the lipid orientation of DMPC bilayers by (31)P solid-state nuclear magnetic resonance (NMR) spectroscopy. Depending on the position of substitution, these peptides adopt mainly either an α-helical structure able to permeabilize DMPC and DMPG vesicles (non-selective peptides) or an intermolecular β-sheet structure only able to permeabilize DMPG vesicles (selective peptides). Several systems have been investigated, namely bilayers mechanically oriented between glass plates as well as bicelles oriented with their normal perpendicular or parallel to the external magnetic field. The results have been compared with spectral simulations with the goal of elucidating the difference in the interaction of these two types of peptides with zwitterionic lipid bilayers. The results indicate that the perturbation induced by selective peptides is much greater than that induced by non-selective peptides in all the lipid systems investigated, and this perturbation has been associated to the aggregation of the selective β-sheet peptides in these systems. On the other hand, the oriented lipid spectra obtained in the presence of non-selective peptides suggest the presence of toroidal pores. This article is part of a Special Issue entitled: Interfacially Active Peptides and Proteins. Guest Editors: William C. Wimley and Kalina Hristova.
authors: Department of Chemistry, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA), Centre québécois sur les matériaux fonctionnels (CQMF), Université Laval, Québec, QC G1V 0A6, Canada.
authors: Matthieu
authors: M
authors: Fillion
authors: Department of Chemistry, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA), Centre québécois sur les matériaux fonctionnels (CQMF), Université Laval, Québec, QC G1V 0A6, Canada.
authors: Mathieu
authors: M
authors: Noël
authors: Department of Chemistry, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA), Centre québécois sur les matériaux fonctionnels (CQMF), Université Laval, Québec, QC G1V 0A6, Canada.
authors: Aurélien
authors: A
authors: Lorin
authors: Department of Chemistry, PROTEO, Université Laval, Québec, QC G1V 0A6, Canada.
authors: Normand
authors: N
authors: Voyer
authors: Department of Chemistry, Regroupement québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Centre de recherche sur les matériaux avancés (CERMA), Centre québécois sur les matériaux fonctionnels (CQMF), Université Laval, Québec, QC G1V 0A6, Canada. Electronic address: michele.auger@chm.ulaval.ca.
authors: Michèle
authors: M
authors: Auger
mesh_terms: D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D010759:Phosphorus Isotopes; D011506:Proteins / Q000737:chemistry*
chemical_list: D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D010455:Peptides; D010759:Phosphorus Isotopes; D011506:Proteins; D004134:Dimyristoylphosphatidylcholine
keywords: Antimicrobial peptides; Nuclear magnetic resonance; Oriented lipid bilayers