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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Antimicrobial Cationic Peptides / chemistry*
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Antimicrobial Cationic Peptides / pharmacology*
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Escherichia coli / chemistry
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Lipopolysaccharides / chemistry*
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Magnetic Resonance Spectroscopy
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Micelles*
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Peptides / chemistry*
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Peptides / pharmacology*
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Polysaccharides, Bacterial / chemistry*
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Protein Conformation
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Salmonella typhimurium / chemistry
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Sequence Homology, Amino Acid
Substances
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Antimicrobial Cationic Peptides
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Lipopolysaccharides
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MSI 594
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Micelles
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Peptides
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Polysaccharides, Bacterial