A solid-state NMR study of changes in lipid phase induced by membrane-fusogenic LV-peptides.
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.
Agrawal
Prashant
P
Biophysical Organic Chemistry/Solid State NMR, LIC, Leiden University, Einsteinweg 55, 2333 CC Leiden, The Netherlands.
Kiihne
Suzanne
S
Hollander
Johan
J
Hofmann
Mathias
M
Langosch
Dieter
D
de Groot
Huub
H
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
D008051:Lipid Bilayers; D050576:Membrane Fusion Proteins; D010455:Peptides