Interactions of two transmembrane peptides in supported lipid bilayers studied by a (31)P and (15)N MAOSS NMR strategy

Biochimie. 2009 Jun;91(6):774-8. doi: 10.1016/j.biochi.2009.01.009.

Abstract

(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%.

MeSH terms

  • Alamethicin / chemistry
  • Alamethicin / metabolism
  • Dimyristoylphosphatidylcholine / chemistry
  • Dimyristoylphosphatidylcholine / metabolism
  • Lipid Bilayers / chemistry
  • Lipid Bilayers / metabolism*
  • Magnetic Resonance Spectroscopy / methods*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Models, Molecular
  • Nitrogen Isotopes
  • Oligopeptides / chemistry
  • Oligopeptides / metabolism
  • Phosphorus Isotopes
  • Protein Binding
  • Protein Structure, Secondary

Substances

  • Lipid Bilayers
  • Membrane Proteins
  • Nitrogen Isotopes
  • Oligopeptides
  • Phosphorus Isotopes
  • Alamethicin
  • Dimyristoylphosphatidylcholine