Binding of Euplotes octocarinatus centrin with target peptide melittin  

作　　者：ZHAO YaQin FENG JiuYing LIANG AiHua YANG BinSheng 

机构地区：[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

出　　处：《Chinese Science Bulletin》2007年第23期3216-3220,共5页

基　　金：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.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 IogKME-EoCen = 6.81±0.33 and Iog-KME-SC-EoCen = 6.51±0.45, respectively.

关 键 词：蜂毒肽 光谱 缩氨酸 生物学 

分 类 号：Q5[生物学—生物化学]