Insights on the Interactions of Synthetic Amphipathic Peptides with Model Membranes as revealed by 31P and 2H Solid-State NMR and Infrared Spectroscopies
Marise Ouellet 1, Geneviéve Bernard 1, Normand Voyer 1 and Michéle Auger 1*
1 Université Laval
* To whom correspondence should be addressed. E-mail: michele.auger{at}chm.ulaval.ca.
Submitted on November 7, 2005
Revised on January 9, 2006
Accepted on 24 February 2006
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Abstract |
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We have 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 have been 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 have been performed on both peptides in interaction with DMPC vesicles in the absence and presence of cholesterol, DMPG 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 while 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 has been 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.
Key Words:
Bicelles, FTIR, Membrane perturbation, Model membranes, Solid-state NMR spectroscopy, Synthetic amphipathic peptides
