Study on the Dynamic Complexation Between Insecticide Fenvalerate and Bovine Serum Albumin

The binding constant is a primary parameter that characterizes molecular-molecular interaction, so the levels of pollutant interaction with receptor may evaluate indirectly the biological toxicity of pollutants. The dynamic complexation between insecticide fenvalerate as a ligand and bovine serum albumin (BSA) as a receptor was measured by affinity capillary electrophoresis (ACE). Both complexation constants was obtained under optimal experimentally condition as follows. 10mmol/L Tris-HCl buffer and pH of 7, capillary column temp. of 25 degrees C, injection time of 5s, injection pressure of 0.5 psi, separation voltage of 15kV and PDA detection wavelength of 214 nm. The mechanism of the interaction between fenvalerate and BSA was discussed. The complexation constant of fenvalerate was compared with typical PAHs, and the strength sequence of complexation of these ligands such as fenvalerate>benzo[a]pyrene>pyrene>phenanthrene.