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Article: Structure-guided optimization of D-captopril for discovery of potent NDM-1 inhibitors

TitleStructure-guided optimization of D-captopril for discovery of potent NDM-1 inhibitors
Authors
KeywordsAntibiotic resistance
Drug discovery
Metallo-β-lactamases (MBLs)
Metallo-β-lactamase inhibitors
Thiol compounds
Issue Date2021
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/bmc
Citation
Bioorganic & Medicinal Chemistry, 2021, v. 29, p. article no. 115902 How to Cite?
Abstractβ-lactam antibiotics have long been the mainstay for the treatment of bacterial infections. New Delhi metallo-β-lactamase 1 (NDM-1) is able to hydrolyze nearly all β-lactam antibiotics and even clinically used serine-β-lactamase inhibitors. The wide and rapid spreading of NDM-1 gene among pathogenic bacteria has attracted extensive attention, therefore high potency NDM-1 inhibitors are urgently needed. Here we report a series of structure-guided design of D-captopril derivatives that can inhibit the activity of NDM-1 in vitro and at cellular levels. Structural comparison indicates the mechanisms of inhibition enhancement and provides insights for further inhibitor optimization.
Persistent Identifierhttp://hdl.handle.net/10722/295505
ISSN
2019 Impact Factor: 3.073
2015 SCImago Journal Rankings: 1.064
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorMa, G-
dc.contributor.authorWang, S-
dc.contributor.authorWu, K-
dc.contributor.authorZhang, W-
dc.contributor.authorAhmad, A-
dc.contributor.authorHao, Q-
dc.contributor.authorLei, X-
dc.contributor.authorZhang, H-
dc.date.accessioned2021-01-25T11:15:50Z-
dc.date.available2021-01-25T11:15:50Z-
dc.date.issued2021-
dc.identifier.citationBioorganic & Medicinal Chemistry, 2021, v. 29, p. article no. 115902-
dc.identifier.issn0968-0896-
dc.identifier.urihttp://hdl.handle.net/10722/295505-
dc.description.abstractβ-lactam antibiotics have long been the mainstay for the treatment of bacterial infections. New Delhi metallo-β-lactamase 1 (NDM-1) is able to hydrolyze nearly all β-lactam antibiotics and even clinically used serine-β-lactamase inhibitors. The wide and rapid spreading of NDM-1 gene among pathogenic bacteria has attracted extensive attention, therefore high potency NDM-1 inhibitors are urgently needed. Here we report a series of structure-guided design of D-captopril derivatives that can inhibit the activity of NDM-1 in vitro and at cellular levels. Structural comparison indicates the mechanisms of inhibition enhancement and provides insights for further inhibitor optimization.-
dc.languageeng-
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/bmc-
dc.relation.ispartofBioorganic & Medicinal Chemistry-
dc.subjectAntibiotic resistance-
dc.subjectDrug discovery-
dc.subjectMetallo-β-lactamases (MBLs)-
dc.subjectMetallo-β-lactamase inhibitors-
dc.subjectThiol compounds-
dc.titleStructure-guided optimization of D-captopril for discovery of potent NDM-1 inhibitors-
dc.typeArticle-
dc.identifier.emailHao, Q: qhao@hku.hk-
dc.identifier.authorityHao, Q=rp01332-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.bmc.2020.115902-
dc.identifier.pmid33302045-
dc.identifier.hkuros320943-
dc.identifier.volume29-
dc.identifier.spagearticle no. 115902-
dc.identifier.epagearticle no. 115902-
dc.identifier.isiWOS:000612171900003-
dc.publisher.placeUnited Kingdom-

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