A Comprehensive Investigation of the Interactions between Proteins and Ligands in the Crystal Structures of Mycobacterium Tuberculosis
Rajesh Nanaware, Anuruddha Chabukswar, Vishal Tekade, Kunal Kashid, Tejas Vidhate, Rushikesh Karmure
Asian Journal of Chemical Sciences · pp. 96–111 · Published 22 Sep 2023
10.9734/ajocs/2023/v13i5257Abstract
Mycobacterium tuberculosis (MTB), an acid-fast aerobic bacterium that may grow on gram stain as either a gram-positive or gram-negative bacterium, is the disease-causing agent of tuberculosis (TB). Rifampin, isoniazid, pyrazinamide and ethambutol, the first-line anti-tubercular drugs, can all have hepatotoxic side effects. The new medicine needs to work through a novel mode of action or to a novel target, be more active than presently available treatments, and shorten the course of treatment for the MDR-TB and XDR-TB, also active against both active and latent bacteria, and does not interact with antiretroviral medications because many TB patients also have HIV. Additionally, it must work well with other anti-TB medications to form at least an effective three-drug regimen. This article discusses the analysis of a few FDA-approved anti-tubercular medications and their binding locations with respective targeted proteins. This mainly focuses on the amino acids of the proteins that are responsible for the formation of interactions with a drug molecule. So, researchers can modify the existing drugs or their derivatives or can construct a new molecule according to the binding sites of enzymes corresponding to mycobacterium tuberculosis.
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