Chem. J. Chinese Universities ›› 2009, Vol. 30 ›› Issue (11): 2175.

• Articles • Previous Articles     Next Articles

Interaction Between Pymetrozine and Bovine Serum Albumin

XU Wei1, WU Xia1*, ZHOU Hai-Ping1, LIU Xiao-Yu1, YANG Jing-He1, FAN Jin-Yong2, ZHANG Mei-Feng2   

  1. 1. School of Chemistry and Chemical Engineering, Shandong University, Jinan 250100, China;
    2. Shandong Pesticide Research Institute, Jinan 250100, China
  • Received:2009-03-04 Online:2009-11-10 Published:2009-11-10
  • Contact: WU Xia. E-mail: wux@sdu.edu.cn
  • Supported by:

    国家自然科学基金(批准号: 20575035)和山东省自然科学基金(批准号: Z2008B04)资助.

Abstract:

The interaction between pymetrozine(Py) and bovine serum albumin(BSA) was investigated by spectroscopy methods, including fluorescence, ultraviolet absorption(UV) and far-UV circular dichroism(CD) spectroscopies. The quenching mechanism of fluorescence was suggested as static quenching according to the Stern-Volmer equation. The thermodynamic parameters enthalpy change(ΔH) and entropy change(ΔS) were calculated, which suggested that the binding power between pymetrozine and bovine serum albumin was hydrogen-bond and van der Waals force. According to the Förster non-radiation energy transfer theory, the binding average distance(r=2.4 nm) between donor(BSA) and acceptor(Py) was obtained. Furthermore, the investigations of the synchromous fluorescence and CD spectra of the system reveal that the conformation of BSA is changed in the presence of Py.

Key words: Pymetrozine; Bovine serum albumin; Fluorescence quenching; Interaction

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