谷胱甘肽对α-芋螺毒素LtIA氧化折叠的影响  

Effect of glutathione on the oxidative folding of synthetic α-conotoxin LtIA

作　　者：王蕊[1] 吴勇[1] 罗素兰[1] 长孙东亭[1] 

机构地区：[1]海南大学热带生物资源教育部重点实验室,海南大学海口市海洋药物重点实验室,海南海口570228

出　　处：《中国海洋药物》2012年第3期17-22,共6页Chinese Journal of Marine Drugs

基　　金：国家自然科学基金(81160503);海南省重点科技计划项目(ZDXM20110040);海南省研究生创新科研课题(Hys2010-9);海南省教育厅高等学校科研项目(Hjkj2010-02);"海南大学211工程创新人才计划项目资助"

摘　　要：目的探究氧化型谷胱甘肽(GSSG)与还原型谷胱甘肽(GSH)不同比例对α-芋螺毒素LtIA氧化折叠过程的影响。方法本实验采用Fmoc固相合成法,合成线性α-芋螺毒素LtIA,而后在Tris-HCl缓冲液中氧化折叠,形成含有天然结构的毒素肽。在氧化折叠过程中,我们设置了氧化型谷胱甘肽与还原型谷胱甘肽不同的比例,观察其对LtIA氧化折叠过程的影响。结果氧化型谷胱甘肽对折叠反应影响明显,能够显著提高折叠反应的速率和产率。结论随着还原型谷胱甘肽比例增加,天然肽的折叠产率有一定程度降低。Objective The effect of the presence and absence of reduced glutathione, oxidized glutathione and different concentration ratios between them on α-conotoxin LtlA folding was investigated. Methods In this study, the linear α-conotoxin LtlA was chemically synthesized using Fmoc solid-phase peptide synthesis protocol, and then it was folded in Tris-HCl buffer. We designed different concentration rati- os between oxidized glutathione and reduced glutathione to observe the effect of the glutathione on α- conotoxin LtIA folding. Results It was indicated that the oxidized glutathione significantly affected the folding reaction, and increased the folding speed and oxidized peptide yield. Conclusion with the reduced glutathione ratio increasing, the folded peptide production was decreased.

关 键 词：谷胱甘肽 氧化折叠 α-芋螺毒素LtIA 

分 类 号：R99[医药卫生—毒理学]