Docking-Based Virtual Screening Ascertaining β-Sitosterol-Induced Alterations in the Helicoverpa armigera Hübner Gut Enzymes

Abstract

Present investigation attempts to study binding of β-sitosterol with Helicoverpa armigera midgut enzymes; alanine aminotransaminase (ALT), aspartate aminotransaminase (AST) and alkaline phosphatase (ALP); through docking-based virtual screening. Extraction of the protein sequence of the enzymes revealed a respective linear chain of 535, 522 and 430 amino acids for ALP, ALT and AST. The binding energy for ALT-ligand complex was lowest as compared to the AST and ALP-docked complexes. The ALT-docked complex had ligand efficiency of (-) 0.32 with an inhibition constant of 104.01, more hydrogen bonds and hydrophobic interactions leading to a more stable complex. However, unfavored bumps in AST and ALP complexes may have led to comparatively unstable complexes. The dietary β-sitosterol exhibits differential binding with midgut enzymes of H. armigera larvae. The strong binding of β-sitosterol with ALT indicates the highest inhibition of ALT activity due to the activity-stability trade-off. The enzymes, AST and ALP exhibited relatively higher activity as a resultant of lesser stabilization of the β-sitosterol-enzyme complex. In silico studies have indicated that β-sitosterol can be used an effective control agent against H. armigera.