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• W1998981711 abstract "In this study, we explored the pharmaceutically underexploited mycobacterial gyrase ATPase (GyrB) domain as a template for a structure-based virtual screening of our in-house (BITS Pilani) compound collection to discover new inhibitors targeting Mycobacterium tuberculosis (M.tb.) The hit identified was further customized by using a combination of molecular docking and medicinal chemistry strategies to obtain an optimized analogue displaying considerable in vitro enzyme efficacy and bactericidal properties against the M.tb. H37Rv strain. The binding affinity of the ligand toward the GyrB domain was reascertained by differential scanning fluorimetry experiments. Further evaluation of the hERG toxicity (a major limitation among the previously reported N-linked aminopiperidine analogues) indicated these molecules to be completely devoid of cardiotoxicity, a significant achievement within this class." @default.
• W1998981711 created "2016-06-24" @default.
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• W1998981711 date "2014-06-23" @default.
• W1998981711 modified "2023-09-26" @default.
• W1998981711 title "Gyrase ATPase Domain as an Antitubercular Drug Discovery Platform: Structure-Based Design and Lead Optimization of Nitrothiazolyl Carboxamide Analogues" @default.
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• W1998981711 doi "https://doi.org/10.1002/cmdc.201402035" @default.
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• W1998981711 hasPublicationYear "2014" @default.
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