Interactions of two transmembrane peptides in supported lipid bilayers studied by a (31)P and (15)N MAOSS NMR strategy.
(31)P and (15)N solid-state NMR with the magic angle-oriented sample spinning (MAOSS) strategy was used to investigate the effect of two model peptides on phospholipid bilayers mimicking biological membrane. One of the peptides, alamethicin, used as a reference of transmembrane alignment, has been shown to disrupt the lipid bilayer organisation, affecting the DMPC packaging. On the other hand, a alpha-helix alanine-rich peptide, K(3)A(18)K(3), with a (15)N labelled alanine, did not present any effect in the DMPC bilayer organisation. The mean orientation of this peptide in the bilayer gave a transmembrane alignment of about 80%.
Kouzayha
Achraf
A
UMR du CNRS, Université de Picardie Jules Verne, Amiens, France.
Wattraint
Olivier
O
Sarazin
Catherine
C
D000408:Alamethicin / Q000737:chemistry / Q000378:metabolism; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry / Q000378:metabolism; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism; D010759:Phosphorus Isotopes; D011485:Protein Binding; D017433:Protein Structure, Secondary
D008051:Lipid Bilayers; D008565:Membrane Proteins; D009587:Nitrogen Isotopes; D009842:Oligopeptides; D010759:Phosphorus Isotopes; D000408:Alamethicin; D004134:Dimyristoylphosphatidylcholine