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  • Title: Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy.
    Author: Bhunia A, Ramamoorthy A, Bhattacharjya S.
    Journal: Chemistry; 2009; 15(9):2036-40. PubMed ID: 19180607.
    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.
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