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dc.contributor.author | Tambe, Pranjali Mahadeo![]() |
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dc.contributor.author | Bhowmick, Shovonlal![]() |
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dc.contributor.author | Chaudhary, Sushil Kumar![]() |
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dc.contributor.author | Khan, Mohammad Rizwan![]() |
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dc.contributor.author | Wabaidur, Saikh M.![]() |
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dc.contributor.author | Muddassir, Mohd.![]() |
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dc.contributor.author | Patil, Preeti Chunarkar![]() |
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dc.contributor.author | Islam, Md Ataul![]() |
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dc.date.accessioned | 2021-11-15T11:10:41Z | |
dc.date.available | 2021-11-15T11:10:41Z | |
dc.date.issued | 2020-12 | |
dc.description.abstract | Tuberculosis (TB) is an infectious disease caused by Mycobacterium tuberculosis (MTB) and considered as serious public health concern worldwide which kills approximately five thousand people every day. Therefore, TB drug development efforts are in gigantic need for identification of new potential chemical agents to eradicate TB from the society. The bacterial DNA gyrase B (GyrB) protein as an experimentally widely accepted effective drug target for the development of TB chemotherapeutics. In the present study, advanced pharmacoinformatics approaches were used to screen the Mcule database against the GyrB protein. Based on a number of chemometric parameters, five molecules were found to be crucial to inhibit the GyrB. A number of molecular binding interactions between the proposed inhibitors and important active site residues of GyrB were observed. The predicted drug-likeness properties of all molecules were indicated that compounds possess characteristics to be the drug-like candidates. The dynamic nature of each molecule was explored through the molecular dynamics (MD) simulation study. Various analyzing parameters from MD simulation trajectory have suggested rationality of the molecules to be potential GyrB inhibitor. Moreover, the binding free energy was calculated from the entire MD simulation trajectories highlighted greater binding free energy values for all newly identified compounds also substantiated the strong binding affection towards the GyrB in comparison to the novobiocin. Therefore, the proposed molecules might be considered as potential anti-TB chemical agents for future drug discovery purposes subjected to experimental validation. | en_ZA |
dc.description.department | Chemical Pathology | en_ZA |
dc.description.librarian | hj2021 | en_ZA |
dc.description.sponsorship | The Researchers Supporting Project through King Saud University, Riyadh, Saudi Arabia. | en_ZA |
dc.description.uri | http://link.springer.com/journal/12010 | en_ZA |
dc.identifier.citation | Tambe, P.M., Bhowmick, S., Chaudhary, S.K. et al. Structure-Based Screening of DNA GyraseB Inhibitors for Therapeutic Applications in Tuberculosis: a Pharmacoinformatics Study. Applied Biochemistry and Biotechnology 192, 1107–1123 (2020). https://doi.org/10.1007/s12010-020-03374-y. | en_ZA |
dc.identifier.issn | 0273-2289 (print) | |
dc.identifier.issn | 1559-0291 (online) | |
dc.identifier.other | 10.1007/s12010-020-03374-y | |
dc.identifier.uri | http://hdl.handle.net/2263/82689 | |
dc.language.iso | en | en_ZA |
dc.publisher | Springer | en_ZA |
dc.rights | © Springer Science+Business Media, LLC, part of Springer Nature 2020. The original publication is available at : http://link.springer.comjournal/12010. | en_ZA |
dc.subject | Tuberculosis (TB) | en_ZA |
dc.subject | DNA GyraseB | en_ZA |
dc.subject | Deoxyribonucleic acid (DNA) | en_ZA |
dc.subject | Virtual screening | en_ZA |
dc.subject | Molecular docking | en_ZA |
dc.subject | Molecular dynamics | en_ZA |
dc.subject.other | Health sciences article SDG-03 | |
dc.subject.other | SDG-03: Good health and well-being | |
dc.title | Structure-based screening of DNA GyraseB inhibitors for therapeutic applications in tuberculosis : a pharmacoinformatics study | en_ZA |
dc.type | Postprint Article | en_ZA |