Citation: DONG Qian, YE Xu-Wen, YANG Jing, WANG Wen-Ming, ZHAO Ya-Qin, YANG Bin-Sheng. Inhibition of Functions for C-Terminal Domain of Euplotes Octocarinatus Centrin by Chlorpromazine Hydrochloride[J]. Chinese Journal of Inorganic Chemistry, ;2021, 37(1): 23-32. doi: 10.11862/CJIC.2021.019 shu

Inhibition of Functions for C-Terminal Domain of Euplotes Octocarinatus Centrin by Chlorpromazine Hydrochloride

  • Corresponding author: YANG Bin-Sheng, yangbs@sxu.edu.cn
  • Received Date: 20 August 2020
    Revised Date: 28 October 2020

Figures(11)

  • The binding of chlorpromazine (CPZ) to the C-terminal domain of Euplotes octocarinatus centrin (apoCEoCen) and the effect of CPZ on the protein function were studied by fluorescence spectra, isothermal titration calorimetry (ITC), circular dichroism (CD) and electrophoresis. The results illustrated that in 10 mmol·L-1 Hepes solution (pH=7.4) at room temperature, CPZ and apoC-EoCen were combined with a molar ratio of 1:1, in addition, the conditional binding constant was about 104 L·mol-1. The combination of CPZ leads to changes in the secondary structure of the protein, and the content of α-helix is reduced. It inhibits the aggregation of centrin induced by metal ions and reduces the fluorescence intensity of Tb3+ sensitization. CPZ suppresses the binding of centrin to xeroderma pigmentosum protein (XPC). The activity of apoC-EoCen nuclease is affected, which results in the decreased capability of protein to cut pBR322 DNA. The results indicate that chlorpromazine hydrochloride is a biological function antagonist of centrin, and it has a good regulatory effect on the function of centrin.
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