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- Publisher
- Wiley
- Copyright
- Copyright © 2009 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 0947-6539
- eISSN
- 1521-3765
- DOI
- 10.1002/chem.200802635
- pmid
- 19180607
- Publisher site
- See Article on Publisher Site
Abstract
Essential understanding: Elucidation of structural requirements and interactions of antimicrobial peptides with lipopolysaccharide (LPS) are essential to understand the mechanism of action of antimicrobial peptides. The highly active antimicrobial peptide MSI‐594 (see figure for electrostatic potential surface) acquires a novel helical hairpin structure in complex with LPS. The structure and interactions of MSI‐594 with LPS presented here provide important insights into the mechanism of outer membrane permeabilization by antimicrobial peptides.
Journal
Chemistry - A European Journal – Wiley
Published: Apr 16, 2010
Keywords: ; ; ;