Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights.
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.
Ramamoorthy
Ayyalusamy
A
Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, USA. ramamoor@umich.edu
D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000494:pharmacology*; D002462:Cell Membrane / Q000737:chemistry / Q000187:drug effects; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*
D023181:Antimicrobial Cationic Peptides