Chemical synthesis and in silico molecular modeling of novel pyrrolyl benzohydrazide derivatives: Their biological evaluation against enoyl ACP reductase (InhA) and Mycobacterium tuberculosis

Antitubercular activity of novel series of pyrrolyl benzohydrazide derivatives was analyzed. and Molecular modeling studied using Surflex-Dock on enoyl ACP reductase from Mycobacterium tuberculosis. [Display omitted] •Synthesis of a range of pyrrolyl benzohydrazide derivatives described.•Surflex docking studies was carried out to understand the binding affinity of the compounds.•Inhibitors were active against Mycobacterium tuberculosis, Staphylococcus aureus, Eschrichia coli, Cell-line (A549) and InhA. In efforts to develop new antitubercular agents, we report here the synthesis of a series of novel pyrrole hydrazine derivatives. The molecules were evaluated against inhibitors of InhA, which is one of the key enzymes involved in type II fatty acid biosynthetic pathway of the mycobacterial cell wall as well as inhibitors of Mycobacterium tuberculosis H37Rv. The binding mode of compounds at the active site of enoyl-ACP reductase was explored using the surflex-docking method. The model suggests one or two H-bonding interactions between the compounds and the InhA enzyme. Some compounds exhibited good activities against InhA in addition to promising activities against M. tuberculosis.