Dynamics and orientation of a cationic antimicrobial peptide in two membrane-mimetic systems.

TitleDynamics and orientation of a cationic antimicrobial peptide in two membrane-mimetic systems.
Publication TypeJournal Article
Year of Publication2010
AuthorsKosol, S., and K. Zangger
JournalJ Struct Biol
Volume170
Issue1
Pagination172-9
Date Published2010 Apr
ISSN1095-8657
KeywordsAntimicrobial Cationic Peptides, Magnetic Resonance Spectroscopy, Membranes, Artificial, Models, Molecular, Nitrogen Isotopes, Phosphorylcholine, Protein Conformation, Protein Folding, Sodium Dodecyl Sulfate
Abstract

In order to investigate the functional and structural properties of cationic alpha-helical peptides in two different membranes, we studied the 20-residue peptide maximin H6 in two membrane-mimetic systems by NMR spectroscopy using partially (15)N-labeled peptide and paramagnetic relaxation enhancements. Maximin H6, which is found in skin secretions of frogs of the Bombinae family, attacks gram-negative bacteria and acts haemolytically. While the peptide spontaneously folds into similar structures in both neutral dodecylphosphocholine (DPC) and negatively charged sodium dodecyl sulphate (SDS) micelles, its structure is more flexible in SDS as shown by (15)N relaxation measurements. In addition, it is bound closer to the surface of the micelle and rotated by approximately 70 degrees around its helix axis in the negatively charged membrane surrogate compared to the structure in DPC. This might form the basis for peptide-peptide interactions through a GxxxG motif, which could finally lead to membrane disruption and, thus, preferential attack of negatively charged microbial cell walls.

DOI10.1016/j.jsb.2009.12.026
Alternate JournalJ. Struct. Biol.
PubMed ID20045466