Investigation of interaction modes involved in alkaline phosphatase and organophosphorus pesticides via molecular simulations

Organophosphorus pesticides (OPPs) are widely used in agricultural production but cause serious pollution. Alkaline phosphatase (ALP) has been implemented to enhance the degradation of OPPs. Deciphering the structural and energetic determinants of OPPs-ALP interaction harbors the potential to understand key biodegradation processes of pesticides at the molecular level. With this aim, the binding modes of OPPs and ALP were studied using computational methods as molecular docking.The CASTp server was used to predict the active site residues. The Discovery Studio Visualizer was used for docking analysis. The results show that OPPs have high binding affinities to ALP with the free energy in the range of−7.68 to−4.06 Kcal mol−1. OPPs and ALP mainly form hydrogen bonds, and amino acid residues, Gln375, Asp55, and Thr413 play important roles in the catalysis process. The experimental data of the OPPs instability in the ALP system is consistent with the binding energy.