The impact of backbone N-methylation on the structure-activity relationship of Leu10-teixobactin

Tony Velkov, James D. Swarbrick, Maytham H. Hussein, Elena K. Schneider-Futschik, Daniel Hoyer, Jian Li, John A. Karas

Research output: Contribution to journalArticleResearchpeer-review

6 Citations (Scopus)


Antimicrobial resistance is a serious threat to global human health; therefore, new anti-infective therapeutics are required. The cyclic depsi-peptide teixobactin exhibits potent antimicrobial activity against several Gram-positive pathogens. To study the natural product's mechanism of action and improve its pharmacological properties, efficient chemical methods for preparing teixobactin analogues are required to expedite structure-activity relationship studies. Described herein is a synthetic route that enables rapid access to analogues. Furthermore, our new N-methylated analogues highlight that hydrogen bonding along the N-terminal tail is likely to be important for antimicrobial activity.

Original languageEnglish
Article numbere3206
Number of pages9
JournalJournal of Peptide Science
Issue number9
Publication statusPublished - Sept 2019

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