Identification of Protease Inhibition Mechanism by Iturin A against Agriculture Cutworm (Spodoptera litura) by Homology Modeling and Molecular Dynamics

Abstract

Spodoptera litura, otherwise known as cutworm, belongs to the Noctuidae tribe, which is a severe scourge for numerous crop systems and is considered one of Asian tropical agriculture's most important insects. The world's leading environmental threats are plant pests, and the already commercialized pesticides are extremely poisonous and non-biodegradable and maybe additional residues harmful to the ecosystem. The increased resistance in pests often demands the need for advanced, active pesticides that are environmentally friendly and biodegradable. In the current work, the significance of proteases for the Spodoptera litura digestive system has been determined by the use of microbial metabolite protease inhibitor (Iturin A) in silico models. In the present study, we developed a model based on sequence structural alignment of known crystal structure 2D1I protease from Homo sapiens. The model's reliability evaluation was performed using programs such as PROCHECK, WHAT IF, PROSA, Validate 3D, ERRAT, etc. In an attempt to find new inhibitors for Protease docking, the study was carried out with Iturin A. PMDB ID for the produced protease model was submitted to identify new inhibitors for Protease docking, and its accession number is PM0082285. The detailed study of enzyme-inhibitor interactions identified similar core residues; GLU215, LEU216, LYS217, and GLU237 have demonstrated their role in the binding efficacy of ligands. The latest homology modeling and docking experiments on the protease model will provide useful insight knowledge for the logical approach of constructing a wide spectrum of novel insecticide against Spodoptera.