Boosting salt resistance of short antimicrobial peptides

Antimicrob Agents Chemother. 2013 Aug;57(8):4050-2. doi: 10.1128/AAC.00252-13. Epub 2013 May 28.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Ampicillin / chemistry
  • Ampicillin / pharmacology*
  • Anti-Infective Agents / chemistry
  • Anti-Infective Agents / pharmacology*
  • Drug Stability
  • Erythrocytes / drug effects
  • Escherichia coli / drug effects
  • Hemolysis
  • Humans
  • Microbial Sensitivity Tests
  • Peptides / chemistry
  • Peptides / pharmacology*
  • Serum / chemistry
  • Sodium Chloride / chemistry*
  • Tryptophan / chemistry
  • beta-Alanine / analogs & derivatives*
  • beta-Alanine / chemistry

Substances

  • Anti-Infective Agents
  • Peptides
  • beta-Alanine
  • Sodium Chloride
  • beta-naphthylalanine
  • Ampicillin
  • Tryptophan