DOI: https://doi.org/10.55373/mjchem.v26i6.58

Keywords: Biovia Discovery Studio; molecular docking; binding affinity; scoring function

Abstract

Organophosphates are widely used as pest control agents in the agriculture industry, as they disrupt the nervous systems of pests. Although they have been used as effective pesticides for many years, their effects on Human Serum Albumin (HSA) has sparked debates over their potential negative impact on the environment and human health. The toxicity of a pesticide is a result of complex formation between a plasma protein, such as serum albumin, and the pesticide. Since these proteins are not encapsulated with carbohydrates, they can easily be bound and transported by various molecules. In this report, the results of a molecular docking experiment focusing on the chemical interactions and scoring function between organophosphate pesticides (OPP) and serum albumin protein via Discovery Studio are described. This study provides a fundamental understanding of the molecular mechanisms underlying their bindings from the interactions via computational analysis. The 2D interactions were able to provide a theoretical foundation for understanding the interaction mechanisms between OPP and Human Serum Albumin (HSA) / Bovine Serum Albumin (BSA). The LIBDOCK and CDOCKER analysis revealed favourable binding with strong intermolecular forces (H-bonds, Van der Waals forces, electrostatic bonds, and hydrophobic effects) between methyl-paraoxon (M-P) with both HSA and BSA. The hydrophobic interactions stabilised M-P inside the active sites of the proteins ALA 291 and ALA 191 in HSA and PHE 550, ALA 527, LEU 574, VAL 575, VAL 546 PHE 506 and LEU 528 in BSA. Structural binding modes showed that hydrophobic interactions play an essential role in stabilizing pesticides inside the active sites of the protein, and the scoring function demonstrated the binding affinities between proteins and pesticides.