Abstract
[structure: see text] Poly(1) kills bacteria (Gram-positive and -negative) and lyses human erythrocytes; this biocidal profile is similar to that of the peptide toxin mellitin. Poly(1) has antibacterial activity comparable to that of a potent derivative of the host defense peptide magainin II, but lacks magainin's selectivity for bacteria over erythrocytes. An analogous N-quaternized polymer, poly(3), is less biocidal than poly(1), suggesting that reversible N-protonation leads to greater biocidal activity than does irreversible N-quaternization.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Anti-Bacterial Agents / chemistry*
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Anti-Bacterial Agents / pharmacology*
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Antimicrobial Cationic Peptides / pharmacology
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Erythrocytes / drug effects
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Humans
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Magainins
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Magnetic Resonance Spectroscopy
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Melitten / pharmacology
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Microbial Sensitivity Tests
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Models, Biological
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Molecular Structure
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Polystyrenes / chemistry*
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Polystyrenes / pharmacology*
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Protons
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Xenopus Proteins / pharmacology
Substances
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Anti-Bacterial Agents
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Antimicrobial Cationic Peptides
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Magainins
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Polystyrenes
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Protons
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Xenopus Proteins
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magainin 2 peptide, Xenopus
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Melitten