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Synergistic transmembrane insertion of the heterodimeric PGLa/magainin 2 complex studied by solid-state NMR

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1788, Issue 8, Pages 1667-1679

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2008.12.018

Keywords

Solid state H-2, N-15 and F-19 NMR; Antimicrobial peptides magainin and PGLa; DMPC and DMPG model membranes; Deuterium quadrupolar splitting; Fluorine homonuclear dipolar coupling; Helix alignment and dynamics

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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 H-2 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-H-2(3)-L-alanine labeled PGLa are included in the analysis. (C) 2009 Elsevier B.V. All rights reserved.

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