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Issue 75, 2018
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Rational design of new cyclic analogues of the antimicrobial lipopeptide tridecaptin A1

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Abstract

Non-ribosomal peptides (NRPs) are a rich source of antibiotic candidates. However, it was recently discovered that resistance to NRPs can be mediated by D-stereoselective peptidases. The tridecaptins, a class of NRPs that selectively target Gram-negative bacteria, are degraded by the D-peptidase TriF. Through analysis of a solution NMR structure of tridecaptin A1, we have rationally synthesized new cyclic tridecaptin analogues that retain strong antimicrobial activity and are resistant to TriF.

Graphical abstract: Rational design of new cyclic analogues of the antimicrobial lipopeptide tridecaptin A1

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Article information


Submitted
17 Jul 2018
Accepted
17 Aug 2018
First published
04 Sep 2018

This article is Open Access

Chem. Commun., 2018,54, 10634-10637
Article type
Communication

Rational design of new cyclic analogues of the antimicrobial lipopeptide tridecaptin A1

R. D. Ballantine, Y. Li, P. Qian and S. A. Cochrane, Chem. Commun., 2018, 54, 10634
DOI: 10.1039/C8CC05790G

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