Chem. J. Chinese Universities ›› 2019, Vol. 40 ›› Issue (11): 2257.doi: 10.7503/cjcu20190334

• Artickes:Chemical Biology • Previous Articles     Next Articles

Binding of Trifluoperazine to N-terminal Domain of Euplotes Octocarinatus Centrin and the Influence on Its Function

YE Xuwen,ZHANG Wenlong,WANG Zhijun,ZHAO Yaqin,YANG Binsheng()   

  1. Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering, Ministry of Education, Shanxi University, Taiyuan 030006, China
  • Received:2019-06-14 Online:2019-11-10 Published:2019-10-15
  • Contact: YANG Binsheng E-mail:yangbs@sxu.edu.cn
  • Supported by:
    ? Supported by the National Natural Science Foundation of China(21571117)

Abstract:

Fluorescence spectroscopy, circular dichroism(CD), isothermal titration calorimetry(ITC), electrophoresis, molecular docking and other modern analytical techniques were used to study the combination of the apoN-terminal domain of Euplotes octocarinatus centrin(apoN-EoCen) with Trifluoperazine(TFP) and observed the effect of TFP on the properties of apoN-EoCen. The results showed that TFP could bind to the E and F helix of the second EF hand of apoN-EoCen and could be combined with a molar ratio of 1∶1 stoichio-metry in 10 mmol/L Hepes buffer solution(pH=7.4) at room temperature. The conditional binding constant is about 10 3 L/mol. The binding of TFP leads to the change of protein secondary structure and the decrease of α-helix content and the decrease of Tb 3+sensitized fluorescence by 83%, and the nuclease activity of apoN-EoCen cleaved DNA is obviously inhibited. Tb 3+ can still occupy the two metal ion binding sites of the protein in the apoN-EoCen-TFP complex, and the conditional binding constant is about 7.0×10 5 L/mol. The bonding of TFP does not inhibit protein aggregation caused by Tb 3+ ions.

Key words: apoN-EoCen, Trifluoperazine, Tb 3+, Spectral analysis

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