In Silico Study of Coumarin Derivatives Against Enoyl ACP Reductase, Ornithine Acetyltransferase and Protein Kinase B Target Enzymes of Mycobacterium tuberculosis

Abstract

Mycobacterium tuberculosis is a bacterial disease that infects and causes tuberculosis (TB) in humans. Millions of people are infected by M. tuberculosis worldwide; so, it is important to have potential drugs against tuberculosis (TB). Mycobacteria have been reported to be multidrug-resistant (MDR-TB) and extensively drug-resistant (XDR-TB) to the available drugs. Enoyl ACP reductase, Ornithine acetyltransferase and Protein kinase B from Mycobacterium tuberculosis are the key enzymes in the survival of M. tuberculosis. So, these enzymes are a potential target. The analysis was performed using an in silico approach to find out docking scores, energy descriptors, ADME/T properties of coumarin derivatives with these targets. Derivatives of coumarins are showing drug likeliness. The molecules are showing binding energy of -9.39 to -8.98 (kcal/mol), -8.266 to -7.419 (kcal/mol) and -9.726 to -8.698 (kcal/mol) with Enoyl ACP reductase, Ornithine acetyltransferase, and Protein kinase B respectively. The docked scores have been compared with standard drug isoniazid and pyrazinamide. The coumarin derivatives have been shown to be potent anti-tubercular agent to MDR-TB.