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New Series of BPL Inhibitors To Probe the Ribose-Binding Pocket of Staphylococcus aureus Biotin Protein Ligase

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العنوان: New Series of BPL Inhibitors To Probe the Ribose-Binding Pocket of Staphylococcus aureus Biotin Protein Ligase
المؤلفون: Sarah Clark, Andrew J. Hayes, Ashleigh S. Paparella, Grant W. Booker, David Heim, Steven W. Polyak, William Tieu, Andrew D. Abell, Jiage Feng
المساهمون: Feng, Jiage, Paparella, Ashleigh S, Tieu, William, Heim, David, Clark, Sarah, Hayes, Andrew, Booker, Grant W, Polyak, Steven W, Abell, Andrew D
المصدر: ACS Medicinal Chemistry Letters. 7:1068-1072
بيانات النشر: American Chemical Society (ACS), 2016.
سنة النشر: 2016
مصطلحات موضوعية: inorganic chemicals, 0301 basic medicine, Staphylococcus aureus, enzyme inhibitors, Binding pocket, Biology, medicine.disease_cause, Biochemistry, antibiotics, 03 medical and health sciences, chemistry.chemical_compound, Biotin, Drug Discovery, Ribose, medicine, biotin protein ligase, Cytotoxicity, chemistry.chemical_classification, DNA ligase, Organic Chemistry, 030104 developmental biology, chemistry, Hepg2 cells, Benzyl group
الوصف: Replacing the labile adenosinyl-substituted phosphoanhydride of biotinyl-5′-AMP with a N1-benzyl substituted 1,2,3-triazole gave a new truncated series of inhibitors of Staphylococcus aureus biotin protein ligase (SaBPL). The benzyl group presents to the ribose-binding pocket of SaBPL based on in silico docking. Halogenated benzyl derivatives (12t, 12u, 12w, and 12x) proved to be the most potent inhibitors of SaBPL. These derivatives inhibited the growth of S. aureus ATCC49775 and displayed low cytotoxicity against HepG2 cells. Refereed/Peer-reviewed
تدمد: 1948-5875
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e60b92eb571193cac10eeb87712df75
https://doi.org/10.1021/acsmedchemlett.6b00248
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....5e60b92eb571193cac10eeb87712df75
قاعدة البيانات: OpenAIRE
الوصف
تدمد:19485875