Synthesis, Molecular Docking and Antibacterial Studies of Novel Azole derivatives as Enoyl ACP Reductase Inhibitor in Escherichia coli. Sindhu T. J.*, Arathi K. N, Devi Akhila, Aswathi T.A., Noushida M., Midhun M., Kuttiyil Sajil Saju Department of Pharmaceutical Chemistry, Sanjo College of Pharmaceutical Studies, Vellappara, Palakkad *Corresponding Author E-mail: sindhutj81@gmail.com
Online published on 3 January, 2020. Abstract The current research is aimed to design of enzyme inhibitors as target for the drug discovery. Azoles can inhibit the enoyl ACP reductase that present in the E. coli is an essential bacterial enzyme. Fabl, the enoyl acyl carrier protein reductase of the Escherichia coli species is one of the attractive targets in E. coli associated diseases. By considering the above observations, an attempt is made here to design and synthesize various N-Mannich bases of azoles as enoyl ACP reductase inhibitors. The synthesized mannich bases were subjected to molecular docking studies with enoyl ACP reductase (PDB ID: 1C14) by using in silico studies by molinspiration online tool. These new compounds were evaluated for their antimicrobial activity. The compounds showed good activity against bacteria Escherichia coli comparable to that of standard drugs Ciprofloxacin. All newly synthesized compounds A1–5 showed antifungal activity towards the tested clinical strain of Escherichia coli. Among these, N-Mannich base compound A3 (benzimidazole derivative) showed good zone of inhibition. In Molecular docking studies, Among the synthesized compounds, diphenylamine derivative of Benzotriazole (A1) has shown binding energy (−5.87 kcal/mol) target protein. Top Keywords Enoyl ACP Reductase Inhibitors, Antimicrobial Activity, Mannich Base, Molecular Docking, Binding Energy. Top |