title: Influence of the mode of insertion of SIV peptides into membranes on the structure of model membrane as studied by 31P NMR.
abstract: The influence on model membrane organization of a fusion peptide of SIV and of a nonfusogenic mutant of this peptide was examined by molecular modeling and by 31P NMR. The calculated mode of insertion of the fusion peptide shows that it adopts an oblique orientation towards the lipid-water interface and that this fusion peptide induces a destabilization of the bilayer structure of multilamellar vesicles as evidenced by 31P NMR observations. The SIV mutant showing a more vertical insertion into lipid layers is unable to induce nonlamellar structures. This study reinforces the correlation between fusogenic activity, induction of structures not organized in extended bilayers, and calculated mode of insertion of peptides into lipid layers.
authors.affiliation: Unité de Chimie Physique Moléculaire et de Cristallographie, Université Catholique de Louvain, Louvain-la-Neuve, Belgium. schanck@cpmc.ucl.ac.be
authors.forename: A
authors.initials: A
authors.lastname: Schanck
authors.forename: J
authors.initials: J
authors.lastname: Peuvot
authors.forename: R
authors.initials: R
authors.lastname: Brasseur
mesh_terms: D000595:Amino Acid Sequence; D009682:Magnetic Resonance Spectroscopy; D008567:Membranes, Artificial; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D010759:Phosphorus Isotopes; D011993:Recombinant Fusion Proteins / Q000737:chemistry*; D015302:Simian Immunodeficiency Virus / Q000737:chemistry*; D014764:Viral Proteins / Q000737:chemistry*
chemical_list: D008567:Membranes, Artificial; D010455:Peptides; D010759:Phosphorus Isotopes; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins