Binding affinity and mechanism of dicofol-lysozyme interaction: Insights from multi-spectroscopy and molecular dynamic simulations.

The pervasive use of dicofol in agricultural settings has been linked to biomolecular perturbations, posing significant threats to environmental sustainability and human health. Therefore, it is crucial to investigate the interactions between dicofol and biomacromolecules, such as proteins. This study employed a range of molecular modeling approaches and spectroscopic techniques to examine the binding interaction between dicofol and lysozyme to elucidate the underlying mechanisms of these toxic effects. Molecular docking studies identified the most optimal binding site for dicofol on the lysozyme structure, highlighting the precise region within the protein where dicofol binds most effectively. Molecular dynamic simulations showed that the dicofol-lysozyme system was stable throughout the entire simulation period. UV-vis absorption and fluorescence emission studies confirmed that dicofol interacts with lysozyme to form a complex. FT-IR analysis revealed that this interaction alters lysozyme's conformation, decreasing alpha-helical content while increasing β-sheet content. Furthermore, a direct relationship was observed between dicofol concentration and lysozyme's activity and stability, with higher dicofol levels causing a notable decline in both factors. In conclusion, this research deepens our understanding of the specific interactions between dicofol and lysozyme while also highlighting the importance of studying such interactions to evaluate the environmental and health risks linked to pesticide usage.