Synergistic transmembrane insertion of the heterodimeric PGLa/magainin 2 complex studied by solid-state NMR.
The skin secretions of amphibians are a rich source of antimicrobial peptides. The two antimicrobial peptides PGLa and magainin 2, isolated from the African frog Xenopus laevis, have been shown to act synergistically by permeabilizing the membranes of microorganisms. In this report, the literature on PGLa is extensively reviewed, with special focus on its synergistically enhanced activity in the presence of magainin 2. Our recent solid state (2)H NMR studies of the orientation of PGLa in lipid membranes alone and in the presence of magainin 2 are described in detail, and some new data from 3,3,3-(2)H(3)-L-alanine labeled PGLa are included in the analysis.
Strandberg
Erik
E
Karlsruhe Institute of Technology, Institute of Biological Interfaces, Forschungszentrum Karlsruhe, P.O.B. 3640, 76021 Karlsruhe, Germany.
Tremouilhac
Pierre
P
Wadhwani
Parvesh
P
Ulrich
Anne S
AS
D000595:Amino Acid Sequence; D000890:Anti-Infective Agents / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D019281:Dimerization; D054806:Magainins; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D029867:Xenopus Proteins / Q000737:chemistry*
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D054806:Magainins; D029867:Xenopus Proteins; C045866:peptide-Gly-Leu-amide; C053301:magainin 2 peptide, Xenopus