Erick J. Dufourc, Sebastien Buchoux, Jeannot Toupe, Marc-Antoine Sani, Frantz Jean-Francois, Lucie Khemtemourian, Axelle Grelard, Cecile Loudet-Courreges, Michel Laguerre, Juan Elezgaray, Bernard Desbat and Benoit Odaert Pages 620 - 631 ( 12 )
Membrane interacting peptides are reviewed in terms of structure and mode of action on lipid membranes. Helical, -stranded, peptides containing both helices and strands, cyclic, lipopeptides and short linear peptides are seen to considerably modulate membrane function. Among peptides that lead to membrane alteration or permeation, antimicrobial peptides play an important role and some of them may be foreseen as potential new antibiotics. Alternatively, peptides that do not destroy the membrane are also very important in modulating the structure and dynamics of the lipid bilayer and play important roles in membrane protein functions. Peptide lipid complexes are shown to be very variable in structure and dynamics: “carpet”, “barrel stave”, toroid and disordered pores, electrostatic wedge and molecular electroporation models are discussed. Their assembly is reviewed in terms of electric, amphipathic and dynamic properties of both lipids and peptides.
Helical-, beta-sheet-, cyclic-, linear-peptides, membrane leakage, membrane reinforcement, membrane crossing, NMR, IR, CD, X-rays, electron microscopy, molecular dynamics.
CBMN, University Bordeaux- CNRS-IPB, Allee Geoffroy St Hilaire, 33600 Pessac, France.