Studies of Interactions between Beta-Cyfluthrin and BSA Based on Fluorescence Spectrometry and Ultraviolet Degradation

Abstract

Pesticides play a pivotal role in modern agriculture, but their potential environmental and health impacts necessitate a comprehensive understanding of their interactions with biological molecules. Beta-cyfluthrin, a widely used synthetic pyrethroid insecticide, is known for its efficiency in pest control. However, its interaction with bovine serum albumin (BSA), a crucial transport protein in living organisms, has not been extensively studied. The interaction between beta-cyfluthrin, a prominent synthetic pyrethroid insecticide, and bovine serum albumin (BSA) was comprehensively investigated using fluorescence spectrometry. Furthermore, the influence of ultraviolet (UV) degradation on the interaction parameters was explored, enhancing our understanding of the impact of environmental conditions on this interaction. The Stern–Volmer equation was employed to determine quenching constants, revealing that the fluorescence quenching mechanism primarily involved static quenching. The temperature variations were studied, showing an increase in the binding constant with rising temperature prior to degradation, while post-UV degradation, an inverse correlation between the binding constant and temperature was observed. The thermodynamic parameters were derived through appropriate equations, unveiling the underlying reaction forces. In the absence of degradation, hydrophobic interactions dominated, whereas after UV degradation, interactions shifted to hydrogen bonding and van der Waals forces. The findings elucidate the nuanced effects of UV degradation on the interaction between beta-cyfluthrin and BSA. This study furnishes critical insights that serve as a scientific foundation for pesticide production and application strategies, accounting for the influence of UV degradation on the intricate interplay between pesticides and BSA.