IN SILICO SCREENING OF VERSATILE PEROXIDASE : A COMPARATIVE ANALYSIS OF BINDING AFFINITY WITH A MIXTURE OF POLLUTANTS USING MOLECULAR DOCKING SIMULATION

Abstract

The infestation of the environment have become an issue across the worldwide due to the mass dissemination of polycyclic aromatic hydrocarbons (PAHs), herbicides, dyes, and endocrine-disrupting compounds, causing sustained environmental impact. Versatile peroxidase is a heme-based ligninolytic biocatalyst secreted by white rot fungi. They have multi-substrate compatibility and assist in the degradation of tenacious environmental toxins. This research employs in-silico molecular docking to broadly analyze the binding affinity of VP and a sample of multiple toxic pollutants, each characterized by their resistance to degradation and ecotoxicity. The three-dimensional structure of VP was designed and assessed followed by computational docking analysis with a provided industrial effluent using PyRx and Vina. Binding affinities, interaction dynamics, and essential catalytic residues were examined to analyze the stability and nature of enzyme pollutant interactions. This comparative analysis also introduces the concept of competitive binding—how the ligands behave with versatile peroxidase in docking of a mixture of pollutants compared to individual docking. This in silico evaluation provides a fundamental understanding of enzyme substrate specificity, promoting ongoing research in biocatalyst development and pollutant degradation.