EMAIL THIS PAGE TO A FRIEND

Biophysical journal

Synergistic insertion of antimicrobial magainin-family peptides in membranes depends on the lipid spontaneous curvature.


PMID 23528099

Abstract

PGLa and magainin 2 (MAG2) are amphiphilic antimicrobial peptides from frog skin with known synergistic activity. The orientation of the two helices in membranes was studied using solid-state (15)N-NMR, for each peptide alone and for a 1:1 mixture of the peptides, in a range of different lipid systems. Two types of orientational behavior emerged. 1), In lipids with negative spontaneous curvature, both peptides remain flat on the membrane surface, when assessed both alone and in a 1:1 mixture. 2), In lipids with positive spontaneous curvature, PGLa alone assumes a tilted orientation but inserts into the bilayer in a transmembrane alignment in the presence of MAG2, whereas MAG2 stays on the surface or gets only slightly tilted, when observed both alone and in the presence of PGLa. The behavior of PGLa alone is identical to that of another antimicrobial peptide, MSI-103, in the same lipid systems, indicating that the curvature-dependent helix orientation is a general feature of membrane-bound peptides and also influences their synergistic intermolecular interactions.

Related Materials

Product #

Image

Description

Molecular Formula

Add to Cart

M7402
Magainin II, ≥97% (HPLC)
C114H180N30O29S
P0053 PGLa
C88H162N26O22S