Refolding of disulfide containing peptides in fusion with thioredoxin

被引：8
|
作者：
Logashina, Yulia A. [1 ,2 ]
Korolkova, Yuliya V. [1 ]
Maleeva, Ekaterina E. [1 ]
Osmakov, Dmitry I. [1 ,2 ]
Kozlov, Sergey A. [1 ]
Andreev, Yaroslav A. [1 ,2 ]
机构：
[1] Russian Acad Sci, MM Shemyakin Yu Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia
[2] IM Sechenov First Moscow State Med Univ, Inst Mol Med, Moscow 119991, Russia
来源：
MENDELEEV COMMUNICATIONS | 2020年 / 30卷 / 02期
基金：
俄罗斯科学基金会;
关键词：
recombinant production; cysteine-rich peptides; refolding; thioredoxin; peptide toxins; SEA-ANEMONE PEPTIDE; ESCHERICHIA-COLI; ANTIMICROBIAL PEPTIDES; BOND FORMATION; EXPRESSION; CHANNEL; APETX2; INHIBITOR; PROTEINS; ASIC3;
D O I：
10.1016/j.mencom.2020.03.028
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
A protocol for refolding of thioredoxin-fused cysteine-rich peptides via addition of oxidized/reduced glutathione reagent directly to unfolded soluble fused protein has been developed. This procedure allows one to skip the steps of inclusion bodies purification, denaturation/disulfide reduction as well as lyophilization before oxidative folding, and thus to improve the yield of cysteine-rich peptides in their production using E. coli expression system.
引用
收藏
页码：214 / 216
页数：3
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