Protein-Ligand interaction analysis of alcohol dehydrogenase from Plutella Xyllostella

Abstract

Plutella Xylostella, (Diamondback Moth) is one of the most destructive insect pests of cruciferous vegetables worldwide. It develops resistance towards synthetic insecticides and possesses a serious threat to the agriculture industry. Introduction of more effective biorational insecticides through integrated pest management (IPM) programs has been proven to reduce the use of chemical pesticides and prevent development of P. Xylostella resistance towards broad-spectrum conventional insecticides. Pheromones have been used in IPM to manipulate the insect behavior to reduce the pest population. An Alcohol Dehydrogenase (ADH) enzyme which involves in the biosynthesis of P. Xylostella sex pheromone has been selected as a good target for biorational insecticide discovery through enzyme inhibition study. The objective of this work is to determine and validate the protein-ligand interaction between P. Xylostella ADH (PxADH) and its ligands; Geraniol, Zn2+ and NADP+. Understanding of this mechanism will provide an insight into the possible catalytic events in the active site, thus may serve as a groundwork for the discovery of more effective analogs and for the establishment of new means of pest management. A 3D homology model of PxADH was constructed to identify the catalytic and coenzyme binding domains. In order to understand the interaction of PxADH with its ligands, a docking analysis of PxADH-Geraniol, PxADH-Zn2+ and PxADH-NADP+ complex was performed using SwissDock. A series of docking were performed to find the most stable binding interaction for the enzyme and its ligands.