Literature DB >> 19272296

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

Erik Strandberg1, Pierre Tremouilhac, Parvesh Wadhwani, Anne S Ulrich.   

Abstract

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.

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Year:  2009        PMID: 19272296     DOI: 10.1016/j.bbamem.2008.12.018

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  26 in total

1.  Knowledge-based computational methods for identifying or designing novel, non-homologous antimicrobial peptides.

Authors:  Davor Juretić; Damir Vukičević; Dražen Petrov; Mario Novković; Viktor Bojović; Bono Lučić; Nada Ilić; Alessandro Tossi
Journal:  Eur Biophys J       Date:  2011-01-28       Impact factor: 1.733

2.  Molecular dynamics simulations on PGLa using NMR orientational constraints.

Authors:  Ulrich Sternberg; Raiker Witter
Journal:  J Biomol NMR       Date:  2015-09-10       Impact factor: 2.835

3.  Charged Antimicrobial Peptides Can Translocate across Membranes without Forming Channel-like Pores.

Authors:  Jakob P Ulmschneider
Journal:  Biophys J       Date:  2017-07-11       Impact factor: 4.033

4.  Oriented samples: a tool for determining the membrane topology and the mechanism of action of cationic antimicrobial peptides by solid-state NMR.

Authors:  Matthieu Fillion; Michèle Auger
Journal:  Biophys Rev       Date:  2015-02-24

5.  Reorientation and dimerization of the membrane-bound antimicrobial peptide PGLa from microsecond all-atom MD simulations.

Authors:  Jakob P Ulmschneider; Jeremy C Smith; Martin B Ulmschneider; Anne S Ulrich; Erik Strandberg
Journal:  Biophys J       Date:  2012-08-08       Impact factor: 4.033

6.  3D hydrophobic moment vectors as a tool to characterize the surface polarity of amphiphilic peptides.

Authors:  Sabine Reißer; Erik Strandberg; Thomas Steinbrecher; Anne S Ulrich
Journal:  Biophys J       Date:  2014-06-03       Impact factor: 4.033

7.  Homo- and heteromeric interaction strengths of the synergistic antimicrobial peptides PGLa and magainin 2 in membranes.

Authors:  Jonathan Zerweck; Erik Strandberg; Jochen Bürck; Johannes Reichert; Parvesh Wadhwani; Olga Kukharenko; Anne S Ulrich
Journal:  Eur Biophys J       Date:  2016-04-06       Impact factor: 1.733

8.  2H-NMR and MD Simulations Reveal Membrane-Bound Conformation of Magainin 2 and Its Synergy with PGLa.

Authors:  Erik Strandberg; Diana Horn; Sabine Reißer; Jonathan Zerweck; Parvesh Wadhwani; Anne S Ulrich
Journal:  Biophys J       Date:  2016-11-15       Impact factor: 4.033

9.  A kinked antimicrobial peptide from Bombina maxima. II. Behavior in phospholipid bilayers.

Authors:  Ralf Heinzmann; Stephan L Grage; Constantin Schalck; Jochen Bürck; Zoltán Bánóczi; Orsolya Toke; Anne S Ulrich
Journal:  Eur Biophys J       Date:  2011-02-11       Impact factor: 1.733

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

Authors:  Erik Strandberg; Jonathan Zerweck; Parvesh Wadhwani; Anne S Ulrich
Journal:  Biophys J       Date:  2013-03-19       Impact factor: 4.033

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