title: A solid-state NMR study of changes in lipid phase induced by membrane-fusogenic LV-peptides.
abstract: Membrane fusion requires restructuring of lipid bilayers mediated by fusogenic membrane proteins. Peptides that correspond to natural transmembrane sequences or that have been designed to mimic them, such as low-complexity "Leu-Val" (LV) peptide sequences, can drive membrane fusion, presumably by disturbing the lipid bilayer structure. Here, we assess how peptides of different fusogenicity affect membrane structure using solid state NMR techniques. We find that the more fusogenic variants induce an unaligned lipid phase component and a large degree of phase separation as observed in (31)P 2D spectra. The data support the idea that fusogenic peptides accumulate PE in a non-bilayer phase which may be critical for the induction of fusion.
authors.affiliation: Biophysical Organic Chemistry/Solid State NMR, LIC, Leiden University, Einsteinweg 55, 2333 CC Leiden, The Netherlands.
authors.forename: Prashant
authors.initials: P
authors.lastname: Agrawal
authors.forename: Suzanne
authors.initials: S
authors.lastname: Kiihne
authors.forename: Johan
authors.initials: J
authors.lastname: Hollander
authors.forename: Mathias
authors.initials: M
authors.lastname: Hofmann
authors.forename: Dieter
authors.initials: D
authors.lastname: Langosch
authors.forename: Huub
authors.initials: H
authors.lastname: de Groot
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D040761:Biomimetic Materials / Q000737:chemistry* / Q000378:metabolism; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism; D008561:Membrane Fusion; D050576:Membrane Fusion Proteins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism
chemical_list: D008051:Lipid Bilayers; D050576:Membrane Fusion Proteins; D010455:Peptides