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Insights on the Interactions of Synthetic Amphipathic Peptides with Model Membranes as Revealed by ³¹P and ²H Solid-State NMR and Infrared Spectroscopies

Département de Chimie, Centre de Recherche sur la Fonction, la Structure et l'Ingénierie des Protéines, Centre de Recherche en Sciences et Ingénierie des Macromolécules, Université Laval, Québec, Québec, Canada

Correspondence: Address reprint requests to Michèle Auger, Département de Chimie, CREFSIP, CERSIM, Université Laval, Québec, Québec, Canada, G1K 7P4. Tel.: 418-656-3393; Fax: 418-656-7916; E-mail: michele.auger{at}chm.ulaval.ca.

We studied the interaction between synthetic amphipathic peptides and model membranes by solid-state NMR and infrared spectroscopies. Peptides with 14 and 21 amino acids composed of leucines and phenylalanines modified by the addition of crown ethers were synthesized. The 14-mer and 21-mer peptides both possess a helical amphipathic structure. To shed light on their membrane interaction, ³¹P and ²H solid-state NMR experiments were performed on both peptides in interaction with dimyristoylphosphatidylcholine vesicles in the absence and presence of cholesterol, dimyristoylphosphatidylglycerol vesicles, and oriented bicelles. ³¹P NMR experiments on multilamellar vesicles reveal that the dynamics and/or orientation of the polar headgroups are weakly yet markedly affected by the presence of the peptides, whereas ³¹P NMR experiments on bicelles indicate no significant changes in the morphology and orientation of the bicelles. On the other hand, ²H NMR experiments on vesicles reveal that the acyl chain order is affected differently depending on the membrane lipidic composition and on the peptide hydrophobic length. Finally, infrared spectroscopy was used to study the interfacial region of the bilayer. Based on these studies, mechanisms of membrane perturbation are proposed for the 14-mer and 21-mer peptides in interaction with model membranes depending on the bilayer composition and peptide length.