Rational design of new cyclic analogues of the antimicrobial lipopeptide tridecaptin A1.
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ABSTRACT:
SUBMITTER: Ballantine RD
PROVIDER: S-EPMC6146376 | biostudies-literature | 2018 Sep
REPOSITORIES: biostudies-literature
Publications
Rational design of new cyclic analogues of the antimicrobial lipopeptide tridecaptin A<sub>1</sub>.
Ballantine Ross D RD Li Yong-Xin YX Qian Pei-Yuan PY Cochrane Stephen A SA
Chemical communications (Cambridge, England) 20180904 75
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 A<sub>1</sub>, we have rationally synthesized new cyclic tridecaptin analogues that retain strong antimicrobial activity and are resistan ...[more]
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