A series of benzimidazole containing isoxazoline-5-one and pyrazoline-5-one compounds were computationally designed and optimized with the Auto Dock 4.0.1 to investigate the interactions between the target compounds and the amino acid residues of the Escherichia coli PDF enzyme and Escherichia coli heptosyltransferase WaaC. In this study, the docking studies were done using auto dock between computationally designed benzimidazole derivatives and peptide deformylase (PDF) and also with heptosyltransferase WaaC. The free energies of binding (? G) and inhibition constants (Ki) of the docked ligands were calculated by the Lamarckian Genetic Algorithm (LGA). These values suggested that the designed benzimidazole derivatives are excellent inhibitor of both Escherichia coli PDF enzyme and heptosyltransferase WaaC.
Keywords: Benzimidazole, isoxazoline-5-one, peptide deformylase and heptosyltransferase WaaC.