Structural highlights
Publication Abstract from PubMed
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.
Helical Hairpin Structure of a Potent Antimicrobial Peptide MSI-594 in Lipopolysaccharide Micelles by NMR Spectroscopy.,Bhunia A, Ramamoorthy A, Bhattacharjya S Chemistry. 2009 Jan 29;15(9):2036-2040. PMID:19180607[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bhunia A, Ramamoorthy A, Bhattacharjya S. Helical Hairpin Structure of a Potent Antimicrobial Peptide MSI-594 in Lipopolysaccharide Micelles by NMR Spectroscopy. Chemistry. 2009 Jan 29;15(9):2036-2040. PMID:19180607 doi:10.1002/chem.200802635
