Insights into the mechanism of interaction between chlordecone and human serum albumin using multiplex spectroscopy and computational methods.

To effectively combat and mitigate the adverse effects associated with the use of bio-based pesticides and to understand their stability in various environmental contexts, it is essential to analyze and fully understand the fundamental characteristics and properties of these complex materials. In this research, a detailed study was conducted to investigate the interaction between chlordecone (CD) and human serum albumin (HSA) under neutral pH conditions. The findings showed that increasing the CD concentration resulted in a significant quenching effect on the static fluorescence emitted by HSA, indicating a significant interaction between the pesticide and the protein. According to thermodynamic analysis and molecular docking data, the binding between CD and HSA primarily occurs within Subdomain IIIB of HSA and is influenced by van der Waals forces, as well as the formation of hydrogen bonds, which play a crucial role in stabilizing the complex. Furthermore, our findings revealed that the presence of CD increased the thermal stability of the protein, a phenomenon that can be attributed to the stabilization of the structural integrity of HSA as a direct result of CD binding. The results obtained from FTIR spectroscopy further confirmed these findings by showing that the presence of CD induces changes in the secondary structure of HSA, leading to structural damage. Furthermore, the use of computational techniques provided further validation of the results obtained through various spectroscopic methods. Taken together, the results of this comprehensive study provide significant insight into the potential health risks that CD may pose to human health.