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

页码：214 / 216

页数：3

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