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

A. Kouzayha (1) , O. Wattraint (1) , C. Sarazin (1)

1 GEC - Génie Enzymatique et Cellulaire

(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%.

Mots clés: Biomimetic membranes; NMR-MAOSS; Alamethicin; Polyalanine peptide; Supported lipid bilayers

Domaines: Sciences du Vivant [q-bio]

A. Kouzayha, O. Wattraint, C. Sarazin. Interactions of two transmembrane peptides in supported lipid bilayers studied by a (31)P and (15)N MAOSS NMR strategy. Biochimie, 2009, 91, pp.774-778. ⟨10.1016/j.biochi.2009.01.009⟩. ⟨hal-00389184⟩