Abstract
The efficacies of many antimicrobial peptides are greatly reduced under high salt concentrations, therefore limiting their use as pharmaceutical agents. Here, we describe a strategy to boost salt resistance and serum stability of short antimicrobial peptides by adding the nonnatural bulky amino acid β-naphthylalanine to their termini. The activities of the short salt-sensitive tryptophan-rich peptide S1 were diminished at high salt concentrations, whereas the activities of its β-naphthylalanine end-tagged variants were less affected.
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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Ampicillin / chemistry
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Ampicillin / pharmacology*
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Anti-Infective Agents / chemistry
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Anti-Infective Agents / pharmacology*
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Drug Stability
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Erythrocytes / drug effects
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Escherichia coli / drug effects
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Hemolysis
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Humans
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Microbial Sensitivity Tests
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Peptides / chemistry
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Peptides / pharmacology*
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Serum / chemistry
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Sodium Chloride / chemistry*
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Tryptophan / chemistry
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beta-Alanine / analogs & derivatives*
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beta-Alanine / chemistry
Substances
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Anti-Infective Agents
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Peptides
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beta-Alanine
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Sodium Chloride
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beta-naphthylalanine
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Ampicillin
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Tryptophan