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Beyond NMR spectra of antimicrobial peptides: Dynamical images at atomic resolution and functional insights

Journal

SOLID STATE NUCLEAR MAGNETIC RESONANCE
Volume 35, Issue 4, Pages 201-207

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ssnmr.2009.03.003

Keywords

Antimicrobial peptides; Membrane; Bilayers; Solid-state NMR

Funding

  1. National Institutes of Health [AI 054515]
  2. American Heart Association [GM 084018]

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There is a considerable current interest in understanding the function of antimicrobial peptides for the development of potent novel antibiotic compounds with a very high selectivity. Since their interaction with the cell membrane is the major driving force for their function, solid-state NMR spectroscopy is the unique method of choice to study these insoluble, non-crystalline, membrane-peptide complexes. Here I discuss solid-state NMR studies of antimicrobial peptides that have reported high-resolution structure, dynamics, orientation, and oligomeric states of antimicrobial peptides in a membrane environment, and also address important questions about the mechanism of action at atomic-level resolution. Increasing number of solid-state NMR applications to antimicrobial peptides are expected in the near future, as these compounds are promising candidates to overcome ever-increasing antibiotic resistance problem and are well suited for the development and applications of solid-state NMR techniques. (C) 2009 Elsevier Inc. All rights reserved.

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