Studies on the interaction between imidacloprid and bovine serum albumin by spectrometry

摘要

The binding studies of imidacloprid to bovine serum albumin (BSA) were investigated by UV-Vis absorption spectrum, fluorescence spectrum and synchronous fluorescence spectrometry. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on BSA and the dynamic quenching constants (K_(sv)) were 6.851×10~4 L·mol~（-1） and 5.813×10~4 L·mol~（-1） at 310 and 315 K, respectively, proving the mode of action of imidacloprid with BSA as a static quenching. In addition, according to the Van't Hoff equation, ΔG~θ <0 showed the combination of imidacloprid and BSA was a spontaneous process; ΔH~θ <0 and ΔS~θ> 0, indicated an electrostatic interaction process. At the same time, synchronous fluorescence spectrum of BSA could tell us whether the conformation of BSA was changed by imidacloprid.