A Comprehensive Investigation of the Interactions between Proteins and Ligands in the Crystal Structures of Mycobacterium Tuberculosis

Abstract

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.