Unknown

Dataset Information

0

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


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.

SUBMITTER: Ballantine RD 

PROVIDER: S-EPMC6146376 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature

altmetric image

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]

Similar Datasets

| S-EPMC5068289 | biostudies-literature
| S-EPMC3904457 | biostudies-literature
| S-EPMC11318538 | biostudies-literature
| S-EPMC10190627 | biostudies-literature
| S-EPMC3047509 | biostudies-literature
| S-EPMC4530663 | biostudies-literature
| S-EPMC1764620 | biostudies-literature
| S-EPMC9204298 | biostudies-literature
| S-EPMC6819921 | biostudies-literature
| S-EPMC6457190 | biostudies-literature