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Article: A discovery of novel Mycobacterium tuberculosis pantothenate synthetase inhibitors based on the molecular mechanism of actinomycin D inhibition

TitleA discovery of novel Mycobacterium tuberculosis pantothenate synthetase inhibitors based on the molecular mechanism of actinomycin D inhibition
Authors
Issue Date2011
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/bmcl
Citation
Bioorganic & Medicinal Chemistry Letters, 2011, v. 21 n. 13, p. 3943-3946 How to Cite?
AbstractMycobacterium tuberculosis pantothenate synthetase is a potential anti-tuberculosis target, and a high-throughput screening system was previously developed to identify its inhibitors. Using a similar system, we screened a small library of compounds and identified actinomycin D (ActD) as a weak inhibitor of pantothenate synthetase. A new method was established to discover more effective inhibitors by determining the molecular mechanism of ActD inhibition followed by structure-based virtual screening. The molecular interaction of inhibition was determined by circular dichroism and tryptophan fluorescence quenching. The structure-based search and virtual screening were performed using the Molecular Operating Environment (MOE) program and SYBYL 7.5, respectively. Two inhibitors were identified with an IC50 for pantothenate synthetase that was at least ten times better than that of ActD
Persistent Identifierhttp://hdl.handle.net/10722/231188
ISSN
2015 Impact Factor: 2.486
2015 SCImago Journal Rankings: 0.952

 

DC FieldValueLanguage
dc.contributor.authorYang, YH-
dc.contributor.authorGao, P-
dc.contributor.authorLiu, YS-
dc.contributor.authorJi, XY-
dc.contributor.authorGan, ML-
dc.contributor.authorGuan, Y-
dc.contributor.authorHao, XQ-
dc.contributor.authorLi, ZR-
dc.contributor.authorXiao, CL-
dc.date.accessioned2016-09-20T05:21:18Z-
dc.date.available2016-09-20T05:21:18Z-
dc.date.issued2011-
dc.identifier.citationBioorganic & Medicinal Chemistry Letters, 2011, v. 21 n. 13, p. 3943-3946-
dc.identifier.issn0960-894X-
dc.identifier.urihttp://hdl.handle.net/10722/231188-
dc.description.abstractMycobacterium tuberculosis pantothenate synthetase is a potential anti-tuberculosis target, and a high-throughput screening system was previously developed to identify its inhibitors. Using a similar system, we screened a small library of compounds and identified actinomycin D (ActD) as a weak inhibitor of pantothenate synthetase. A new method was established to discover more effective inhibitors by determining the molecular mechanism of ActD inhibition followed by structure-based virtual screening. The molecular interaction of inhibition was determined by circular dichroism and tryptophan fluorescence quenching. The structure-based search and virtual screening were performed using the Molecular Operating Environment (MOE) program and SYBYL 7.5, respectively. Two inhibitors were identified with an IC50 for pantothenate synthetase that was at least ten times better than that of ActD-
dc.languageeng-
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/bmcl-
dc.relation.ispartofBioorganic & Medicinal Chemistry Letters-
dc.rightsPosting accepted manuscript (postprint): © <year>. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/-
dc.titleA discovery of novel Mycobacterium tuberculosis pantothenate synthetase inhibitors based on the molecular mechanism of actinomycin D inhibition-
dc.typeArticle-
dc.identifier.emailGao, P: gaopeng@hku.hk-
dc.identifier.doi10.1016/j.bmcl.2011.05.021-
dc.identifier.hkuros266397-
dc.identifier.volume21-
dc.identifier.issue13-
dc.identifier.spage3943-
dc.identifier.epage3946-
dc.publisher.placeUnited Kingdom-

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