title: Comparative interaction of alpha-helical and beta-sheet amphiphilic isopeptides with phospholipid monolayers.
abstract: The two sequential amphiphilic peptide isomers, (Leu-Lys-Lys-Leu)4 and (Leu-Lys)8, were chosen as models for alpha-helical and beta-sheet peptides, respectively. In order to evaluate the contribution of the secondary structure of a peptide to its penetration into cellular membranes, interactions of these isopeptides with L-alpha-dimyristoyl phosphatidylcholine (DMPC) monolayers were studied. Both isopeptides penetrate into DMPC monolayers up to an exclusion pressure of approximately 27 mN/m, but a discontinuity is observed in the penetration profile of the alpha-helical (LKKL)4. The main parameters extracted from the compression isotherms of the mixed peptide/DMPC monolayers-namely, transition pressure, mean area, elasticity modulus, and energy of mixing-were analyzed. These analyses indicate that the alpha-helical isomer interacts strongly with DMPC by forming a 1:32 (LKKL)4-DMPC complex. When engaged in this complex, (LKKL)(4) behaves as an hydrophobic helix and has a tendency to become vertically oriented in the course of the compression process. The beta-sheet (LK)8 interacts more weakly with DMPC and no complex can be detected.
authors.affiliation: Centre de Biophysique Moléculaire (CNRS) rue Charles-Sadron, 45071 Orléans Cedex 2, France. maget@cnrs-orleans.fr
authors.forename: R
authors.initials: R
authors.lastname: Maget-Dana
authors.forename: D
authors.initials: D
authors.lastname: Lelièvre
mesh_terms: D004134:Dimyristoylphosphatidylcholine / Q000378:metabolism; D008567:Membranes, Artificial; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013501:Surface-Active Agents / Q000737:chemistry* / Q000378:metabolism
chemical_list: D008567:Membranes, Artificial; D010455:Peptides; D013501:Surface-Active Agents; D004134:Dimyristoylphosphatidylcholine