Synthesis and structure-activity relationship studies of N-terminal analogues of the antimicrobial peptide tridecaptin A(1)

Stephen A Cochrane, Christopher T Lohans, Jeremy R Brandelli, George Mulvey, Glen D Armstrong, John C Vederas

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)

Abstract

Chemical synthesis was used to increase the potency of the antimicrobial lipopeptide tridecaptin A1. Lipid tail modification proved to be an ideal platform for synthesizing structurally simpler analogues that are not readily accessible by isolation. The stereochemical elements of the tridecaptin A1 lipid tail are not essential for antimicrobial activity and could be replaced with hydrophobic aliphatic or aromatic groups. Some simpler analogues displayed potent antimicrobial activity against Gram-negative bacteria, including Campylobacter jejuni, Escherichia coli O157:H7, and multidrug resistant Klebsiella pneumoniae.

Original languageEnglish
Pages (from-to)1127-31
JournalJournal of Medicinal Chemistry
Volume57
Issue number3
Early online date30 Jan 2014
DOIs
Publication statusPublished - 13 Feb 2014

Keywords

  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Drug Resistance, Bacterial
  • Gram-Negative Bacteria
  • Hemolysis
  • Hydrophobic and Hydrophilic Interactions
  • Lipopeptides
  • Peptides
  • Stereoisomerism
  • Structure-Activity Relationship
  • Journal Article
  • Research Support, Non-U.S. Gov't

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