STUDY OF STRUCTURE BASED DESIGN FOR SULFONES AS ENOYL-ACP REDUCTASE INHIBITORS

Mycobacterium leprae, the causative agent of the disease, leprosy develops resistance against most of the drugs, so novel drug targets are required to design new drugs. Present work is aimed at understanding the inhibition of enoyl-acyl carrier protein reductase (Enoyl-ACP reductase), which is one of the receptor proteins used in drug discovery for screening anti-leprosy agents by virtually designed sulfone class of compounds. The crystal structure of the inhibited M. leprae InhA complex (2NTV) provides the details of protein-ligand interactions. The virtually designed series of compounds having sulfone moiety have docked well in the active site region of the protein. The prediction of ADME properties was also performed by Qikprop software. Mycobacterium leprae, the causative agent of the disease, leprosy develops resistance against most of the drugs, so novel drug targets are required to design new drugs. Present work is aimed at understanding the inhibition of enoyl-acyl carrier protein reductase (Enoyl-ACP reductase), which is one of the receptor proteins used in drug discovery for screening anti-leprosy agents by virtually designed sulfone class of compounds. The crystal structure of the inhibited M. leprae InhA complex (2NTV) provides the details of protein-ligand interactions. The virtually designed series of compounds having sulfone moiety have docked well in the active site region of the protein. The prediction of ADME properties was also performed by Qikprop software candidates.