吴勇,徐盼,任洁,等.α-芋螺毒素TxIB氧化折叠路径研究[J].中国海洋药物,2016,35(4):65-70.
α-芋螺毒素TxIB氧化折叠路径研究
Pathway of Oxidative Folding of α-Conotoxin TxIB
投稿时间:2015-12-07  修订日期:2016-01-25
DOI:
中文关键词:  α-芋螺毒素TxIB  固相多肽合成  切割  氧化折叠路径
English Keywords:α-conotoxin TxIB  solid phase peptide synthesis  cleavage  pathway of oxidative folding
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作者单位E-mail
吴勇 生物技术实验中心 3046633@qq.com 
徐盼 生物技术实验中心  
任洁 生物技术实验中心  
长孙东亭 生物技术实验中心  
罗素兰* 生物技术实验中心 luosulan2003@163.com 
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中文摘要:
      目的:阐明TxIB线性肽通过一部氧化法,在体外被氧化折叠形成含有两对二硫键活性肽的具体路径,为后续大量人工合成该活性肽的方法研究提供基础。方法 采用N-9芴甲氧羰基(Fmoc)固相合成法人工合成TxIB线性肽,用高效液相和质谱分析法,监测研究TxIB一步氧化折叠过程中所经历的路径。结果 TxIB氧化路径经历了1对二硫键(1SS)、2对二硫键(X-2SS)折叠中间体后,最终形成稳定的含有2对二硫键(N-2SS)的氧化型TxIB。结论芋螺毒素TxIB折叠路径与前期研究的水蛭素氧化折叠路径一致。
English Summary:
      Objective To elucidate one-step oxidative folding pathway of linear TxIB peptide, and to give a guidance to synthesize peptide TxIB in large amounts. Methods Linear TxIB was synthesized by solid-phase synthesis method, and the pathway of oxidative folding was monitored and determined by reverse phase high performance liquid chromatography and mass spectrometry analysis. Results The folding intermediates of reduced TxIB had one disulfide bond (1SS), two disulfide bonds (X-2SS), and formed the active TxIB peptide with two stable disulfide bonds (N-2SS) finally. Conclusion The pathway of oxidative folding of peptide TxIB exhibited a high degree of similarity to hirudin.
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