Studies on the interaction between imidacloprid and human serum albumin:Spectroscopic approach

摘要

The interaction between imidacloprid(IMI)and human serum albumin(HSA)was investigated using fluorescence and UV/vis absorption spectroscopy.The experimental results showed that the fluorescence quenching of HSA by IMI was a result of the formation of IMI-HSA complex;static quenching was confirmed to result in the fluorescence quenching.The apparent binding constant K_A between IMI and HSA at three differences were obtained to be 1.51 X 10~4,1.58 X 10~4,and 2.19 X 10~4 L mol~(-1)respectively.The thermodynamic parameters,DELTA H~o and DELT S~o were estimated to be 28.44 kJ mol~(-1),174.76 Jmol~(-1) K~(-1)according to the van't Hoff equation.Hydrophobic interactions played a major role in stabilizing the complex.The distance r between donor(HSA)and acceptor(IMI)was obtained according to fluorescence resonance energy transfer.The effect of IMI on the conformation of HSA was analyzed using synchronous fluorescence spectroscopy CD and three-dimensional fluorescence spectra,the environment around Trp and Tyr residues were altered.