This article is cited in 10 papers

Communications

Refolding of disulfide containing peptides in fusion with thioredoxin

Yu. A. Logashina^ab, Yu. V. Korolkova^a, E. E. Maleeva^a, D. I. Osmakov^ab, S. A. Kozlov^a, Ya. A. Andreev<sup>ab

a</sup> M.M. Shemyakin–Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russian Federation
^b I.M. Sechenov First Moscow State Medical University, Moscow, Russian Federation

Abstract: 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.

Keywords: recombinant production, cysteine-rich peptides, refolding, thioredoxin, peptide toxins.

Language: English

DOI: 10.1016/j.mencom.2020.03.028

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