Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy.
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.
Bhunia
Anirban
A
School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore.
Ramamoorthy
Ayyalusamy
A
Bhattacharjya
Surajit
S
D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000494:pharmacology*; D004926:Escherichia coli / Q000737:chemistry; D008070:Lipopolysaccharides / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology*; D011135:Polysaccharides, Bacterial / Q000737:chemistry*; D011487:Protein Conformation; D012486:Salmonella typhimurium / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D023181:Antimicrobial Cationic Peptides; D008070:Lipopolysaccharides; C511193:MSI 594; D008823:Micelles; D010455:Peptides; D011135:Polysaccharides, Bacterial