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

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

doi:10.1039/c8cc05790g

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

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

School of Chemistry and Chemical Engineering

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

237 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 language	English
Pages (from-to)	1-4
Journal	Chemical Communications
Early online date	04 Sept 2018
DOIs	https://doi.org/10.1039/c8cc05790g
Publication status	Early online date - 04 Sept 2018

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10.1039/c8cc05790gLicence: CC BY

Rational design of new cyclic analogues of the antimicrobial lipopeptide tridecaptin A1†
Copyright 2018 the authors. This is an open access article published under a Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
Final published version, 1.95 MBLicence: CC BY

Structural and mechanistic studies on antimicrobial peptides that target multi-drug resistant bacteria
Ballantine, R. (Author), Cochrane, S. (Supervisor) & Stevenson, P. (Supervisor), Jul 2021
Student thesis: Doctoral Thesis › Doctor of Philosophy

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Stephen Cochrane
- s.cochranequb.acuk
Person: Academic

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

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Structural and mechanistic studies on antimicrobial peptides that target multi-drug resistant bacteria

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Stephen Cochrane

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