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Article: Rational design of new cyclic analogues of the antimicrobial lipopeptide tridecaptin A1

TitleRational design of new cyclic analogues of the antimicrobial lipopeptide tridecaptin A1
Authors
Ballantine, Ross D.Li, Yong XinQian, Pei YuanCochrane, Stephen A.
Issue Date2018
Citation
Chemical Communications, 2018, v. 54, n. 75, p. 10634-10637 How to Cite?
DOI: http://dx.doi.org/10.1039/c8cc05790g
Abstract© 2018 The Royal Society of Chemistry. 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.
Persistent Identifierhttp://hdl.handle.net/10722/273638
ISSN
1359-7345
2023 Impact Factor: 4.3
2023 SCImago Journal Rankings: 1.133
ISI Accession Number ID
WOS:000444811200023

 

DC FieldValueLanguage
dc.contributor.authorBallantine, Ross D.-
dc.contributor.authorLi, Yong Xin-
dc.contributor.authorQian, Pei Yuan-
dc.contributor.authorCochrane, Stephen A.-
dc.date.accessioned2019-08-12T09:56:13Z-
dc.date.available2019-08-12T09:56:13Z-
dc.date.issued2018-
dc.identifier.citationChemical Communications, 2018, v. 54, n. 75, p. 10634-10637-
dc.identifier.issn1359-7345-
dc.identifier.urihttp://hdl.handle.net/10722/273638-
dc.description.abstract© 2018 The Royal Society of Chemistry. 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.-
dc.languageeng-
dc.relation.ispartofChemical Communications-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleRational design of new cyclic analogues of the antimicrobial lipopeptide tridecaptin A1-
dc.typeArticle-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1039/c8cc05790g-
dc.identifier.pmid30179243-
dc.identifier.scopuseid_2-s2.0-85053559465-
dc.identifier.volume54-
dc.identifier.issue75-
dc.identifier.spage10634-
dc.identifier.epage10637-
dc.identifier.eissn1364-548X-
dc.identifier.isiWOS:000444811200023-
dc.identifier.issnl1359-7345-

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