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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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Publication details

The article was received on 17 Jul 2018, accepted on 17 Aug 2018 and first published on 04 Sep 2018


Article type: Communication
DOI: 10.1039/C8CC05790G
Citation: Chem. Commun., 2018,54, 10634-10637
  • Open access: Creative Commons BY license
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    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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