Paper Title
Molecular Docking Study of Nitrothiazole Derivatives to Develop The Gyrb Inhibitors

Abstract
Tuberculosis caused by Mycobacterium tuberculosis (M. tuberculosis) is the cause of death worldwide.DNA gyrasehas been identified as promising target for anti-tuberculosis development. This enzyme is the binding pocket of quinolones, the drug for anti-tuberculosis agents. However, quinolones used to treat MDR-TB is debatable due to association about emerging resistance in M. tuberculosis. Nitrothiazole derivatives were designed as new GyrB inhibitors of DNA gyrase with moderate activities against GyrB and mycobacterial cell. In the present study, we aim to develop new highly potent GyrB inhibitors based on nitrothiazolederivatives. Molecular docking calculations were used to elucidate the key interactions for binding of these inhibitors in GyrB binding pocket. The obtained results showed that hydrogen bond interaction between ligand and Glu48, Val49, Asn52, Val77, Asp79, Arg82, Gly83, Ile84, Gly107, Lys108, Tyr114, Gly119, Leu120, His121, Gly122, Gly124, Arg141 and Lys372 residues were crucial interactions. Moreover, cation-pi interaction was improved the binding affinity of inhibitors in GyrB binding site. The integrated results from docking in this work aid to rational design new and more potent GyrB inhibitors in a series of nitrothiazole as novel anti-tuberculosis agents. Keywords - Gyrase B, Molecular docking calculations, Binding pocket, Amino acid