Abstract
The horseshoe crab peptide polyphemusin I possesses high antimicrobial activity, but its mechanism of action is as yet not well defined. Using a biotin-labeled polyphemusin I analogue and confocal fluorescence microscopy, we showed that the peptide accumulates in the cytoplasm of wild-type Escherichia coli within 30 min after addition without causing substantial membrane damage.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Anti-Bacterial Agents / pharmacology*
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Antimicrobial Cationic Peptides / metabolism
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Antimicrobial Cationic Peptides / pharmacology*
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Cytoplasm / metabolism*
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Escherichia coli / drug effects*
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Escherichia coli / metabolism
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Molecular Sequence Data
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Octoxynol / pharmacology
Substances
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Anti-Bacterial Agents
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Antimicrobial Cationic Peptides
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polyphemusin I
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Octoxynol