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Helical Hairpin Structure of a Potent Antimicrobial Peptide MSI-594 in Lipopolysaccharide Micelles by NMR Spectroscopy

✍ Scribed by Anirban Bhunia; Ayyalusamy Ramamoorthy; Surajit Bhattacharjya

Book ID: 102795102
Publisher: John Wiley and Sons
Year: 2009
Tongue: English
Weight: 656 KB
Volume: 15
Category: Article
ISSN: 0947-6539
DOI: 10.1002/chem.200802635

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✦ Synopsis

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.magnified image

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