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Binding of Euplotes octocarinatus centrin with target peptide melittin
作者单位:ZHAO YaQin(Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan 030006, China) ; FENG JiuYing(Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan 030006, China) ; LIANG AiHua (Institute of Biotechnology, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan 030006, China) ; YANG BinSheng(Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan 030006, China) ;
基金项目:Supported by the National Natural Science Foundation of China (Grant Nos. 20371031 and 20771068),the Natural Science Foundation of Shanxi Province (Grant No. 2007011024),Young Science Foundation of Shanxi University
摘    要:Interactions between model target peptide melittin (ME) and Euplotes octocarinatus centrin (EoCen) were investigated by fluorescence spectra, circular dichroism (CD) spectra and native polyacrylamide gel electrophoresis (PAGE). In 0.1 mol/L N-2-hydroxyethylpiperazine-N-2-ethanesulfonic acid (Hepes) and 150 mmol/L NaCl at pH 7.4, EoCen and isolated short C-terminal domain of EoCen (SC-EoCen) form 1:1 peptide:protein complexes. However, no detectable signal changes can be observed while isolated N-terminal domain of EoCen (N-EoCen) or isolated long C-terminal domain of EoCen (LC-EoCen) was added into solution of ME. The interaction between EoCen and ME is specified exclusively for the short C-terminal domain of EoCen. On the basis of fluorescence titration curves, the conditional binding constants of ME with EoCen and SC-EoCen were calculated to be logKME-EoCen = 6.81±0.33 and log- KME-SC-EoCen = 6.51±0.45, respectively.

关 键 词:蜂毒肽  光谱  缩氨酸  生物学
收稿时间:2007-02-01
修稿时间:2007-04-13

Binding of Euplotes octocarinatus centrin with target peptide melittin
Authors:YaQin Zhao  JiuYing Feng  AiHua Liang  BinSheng Yang
Institution:(1) Institute of Molecular Science, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan, 030006, China;(2) Institute of Biotechnology, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan, 030006, China
Abstract:Interactions between model target peptide melittin (ME) and Euplotes octocarinatus centrin (EoCen) were investigated by fluorescence spectra, circular dichroism (CD) spectra and native polyacrylamide gel electrophoresis (PAGE). In 0.1 mol/L N-2-hydroxyethylpiperazine-N-2-ethanesulfonic acid (Hepes) and 150 mmol/L NaCl at pH 7.4, EoCen and isolated short C-terminal domain of EoCen (SC-EoCen) form 1:1 peptide: protein complexes. However, no detectable signal changes can be observed while isolated N-terminal domain of EoCen (N-EoCen) or isolated long C-terminal domain of EoCen (LC-EoCen) was added into solution of ME. The interaction between EoCen and ME is specified exclusively for the short C-terminal domain of EoCen. On the basis of fluorescence titration curves, the conditional binding constants of ME with EoCen and SC-EoCen were calculated to be logK ME-EoCen = 6.81±0.33 and logK ME-SC-EoCen = 6.51±0.45, respectively. Supported by the National Natural Science Foundation of China (Grant Nos. 20371031 and 20771068), the Natural Science Foundation of Shanxi Province (Grant No. 2007011024) and Young Science Foundation of Shanxi University
Keywords:centrin  melittin  spectra
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