Rational Design of New Cyclic Analogues of the Antimicrobial Lipopeptide Tridecaptin A1

Ross Ballantine, Yong-Xin Li, Pei-Yuan Qian, Stephen Cochrane

Research output: Contribution to journalArticle

7 Citations (Scopus)
115 Downloads (Pure)

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.
Original languageEnglish
Pages (from-to)1-4
JournalChemical Communications
Early online date04 Sep 2018
DOIs
Publication statusEarly online date - 04 Sep 2018

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Lipopeptides
proline dipeptidase
Peptides
Antibiotics
Bacteria
Nuclear magnetic resonance
Anti-Bacterial Agents
tridecaptins
Peptide Hydrolases

Cite this

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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.",
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Rational Design of New Cyclic Analogues of the Antimicrobial Lipopeptide Tridecaptin A1. / Ballantine, Ross; Li, Yong-Xin; Qian, Pei-Yuan; Cochrane, Stephen.

In: Chemical Communications, 04.09.2018, p. 1-4.

Research output: Contribution to journalArticle

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AU - Ballantine, Ross

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AU - Qian, Pei-Yuan

AU - Cochrane, Stephen

PY - 2018/9/4

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AB - 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.

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