Molecular insights into the interaction between myoglobin and Imidacloprid: Multi-spectral experiments and computational simulations

Abstract

Imidacloprid (IMI) belongs to the neonicotinoid insecticides, specifically the imidazole chemical group, which exhibits a high level of contact, digestive, and systemic effects on the central nervous system of insects. In this study, we investigated the impact of IMI on the conformation and structural stability of myoglobin (Mb) protein using spectroscopic techniques combined with molecular docking and simulation approaches. Additionally, we examined the thermal stability of the resulting complex. The UV–Visible results demonstrated the interaction between IMI and Mb protein. The intrinsic fluorescence of Mb was effectively quenched by IMI, indicating successful binding and the formation of a stable complex. Thermodynamic analysis revealed that the spontaneous bonding process was primarily governed by van der Waals forces and hydrogen bonds. FT-IR analysis indicated that IMI induced conformational changes in Mb, providing further evidence of its potential toxicity and structural damage to Mb. Furthermore, the interaction significantly enhanced the thermal stability of Mb compared to Mb alone. Molecular docking revealed the preferred binding site of IMI within the Mb structure. Molecular dynamics (MD) simulation results further supported the findings by demonstrating a decrease in compactness and an increase in the stability of the Mb-IMI complex. These findings offer valuable insights into the potential toxicity risks of IMI to human health and shed light on the binding mechanism between IMI and Mb. The results of this study serve as a useful model for gaining a deeper understanding of the effects of these pesticides on proteins and body health.