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Article: A Chemical-Intervention Strategy To Circumvent Peptide Hydrolysis by d-Stereoselective Peptidases

TitleA Chemical-Intervention Strategy To Circumvent Peptide Hydrolysis by d-Stereoselective Peptidases
Authors
KeywordsLipids
Peptides and proteins
Antimicrobial activity
Hydrolysis
Assays
Issue Date2019
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/jmc
Citation
Journal of Medicinal Chemistry, 2019, v. 62 n. 22, p. 10466-10472 How to Cite?
AbstractD-Stereoselective peptidases that degrade nonribosomal peptides (NRPs) were recently discovered and could have serious implications for the future of NRPs as antibiotics. Herein, we report chemical modifications that can be used to impart resistance to the d-peptidases BogQ and TriF. New tridecaptin A analogues were synthesized that retain strong antimicrobial activity and have significantly enhanced d-peptidase stability. Invitro assays confirmed that synthetic analogues retain the ability to bind to their cellular receptor, peptidoglycan intermediate lipid II.
Persistent Identifierhttp://hdl.handle.net/10722/284013
ISSN
2020 Impact Factor: 7.446
2015 SCImago Journal Rankings: 2.529
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBann, SJ-
dc.contributor.authorBallantine, RD-
dc.contributor.authorMcCallion, CE-
dc.contributor.authorQian, PY-
dc.contributor.authorLi, YX-
dc.contributor.authorCochrane, SA-
dc.date.accessioned2020-07-20T05:55:19Z-
dc.date.available2020-07-20T05:55:19Z-
dc.date.issued2019-
dc.identifier.citationJournal of Medicinal Chemistry, 2019, v. 62 n. 22, p. 10466-10472-
dc.identifier.issn0022-2623-
dc.identifier.urihttp://hdl.handle.net/10722/284013-
dc.description.abstractD-Stereoselective peptidases that degrade nonribosomal peptides (NRPs) were recently discovered and could have serious implications for the future of NRPs as antibiotics. Herein, we report chemical modifications that can be used to impart resistance to the d-peptidases BogQ and TriF. New tridecaptin A analogues were synthesized that retain strong antimicrobial activity and have significantly enhanced d-peptidase stability. Invitro assays confirmed that synthetic analogues retain the ability to bind to their cellular receptor, peptidoglycan intermediate lipid II.-
dc.languageeng-
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/jmc-
dc.relation.ispartofJournal of Medicinal Chemistry-
dc.rightsThis document is the Accepted Manuscript version of a Published Work that appeared in final form in [JournalTitle], copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see [insert ACS Articles on Request author-directed link to Published Work, see http://pubs.acs.org/page/policy/articlesonrequest/index.html].-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectLipids-
dc.subjectPeptides and proteins-
dc.subjectAntimicrobial activity-
dc.subjectHydrolysis-
dc.subjectAssays-
dc.titleA Chemical-Intervention Strategy To Circumvent Peptide Hydrolysis by d-Stereoselective Peptidases-
dc.typeArticle-
dc.identifier.emailLi, YX: yxpli@hku.hk-
dc.identifier.authorityLi, YX=rp02556-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1021/acs.jmedchem.9b01078-
dc.identifier.pmid31657913-
dc.identifier.pmcidPMC6887851-
dc.identifier.scopuseid_2-s2.0-85074939521-
dc.identifier.hkuros310994-
dc.identifier.volume62-
dc.identifier.issue22-
dc.identifier.spage10466-
dc.identifier.epage10472-
dc.identifier.isiWOS:000500420100030-
dc.publisher.placeUnited States-
dc.identifier.issnl0022-2623-

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