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Solid State Nucl Magn Reson. 2009 Jul;35(4):201-7. doi: 10.1016/j.ssnmr.2009.03.003. Epub 2009 Mar 31.

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

Author information

1
Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, USA. ramamoor@umich.edu

Abstract

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.

PMID:
19386477
PMCID:
PMC2694728
DOI:
10.1016/j.ssnmr.2009.03.003
[Indexed for MEDLINE]
Free PMC Article

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