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Refolding of disulfide containing peptides in fusion with thioredoxin

Yulia A. Logashina 1, 2
Yulia A. Logashina
Yuliya Vladimirovna Korolkova 1
Yuliya Vladimirovna Korolkova
Ekaterina Evgenievna Maleeva 1
Ekaterina Evgenievna Maleeva
Dmitry Igorevich Osmakov 1, 2
Dmitry Igorevich Osmakov
Sergei Aleksandrovich Kozlov 1
Sergei Aleksandrovich Kozlov
Yaroslav Alekseevich Andreev 1, 2
Yaroslav Alekseevich Andreev
Published 2020-03-02
CommunicationVolume 30, Issue 2, 214-216
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Logashina Y. A. et al. Refolding of disulfide containing peptides in fusion with thioredoxin // Mendeleev Communications. 2020. Vol. 30. No. 2. pp. 214-216.
GOST all authors (up to 50) Copy
Logashina Y. A., Korolkova Y. V., Maleeva E. E., Osmakov D. I., Kozlov S. A., Andreev Y. A. Refolding of disulfide containing peptides in fusion with thioredoxin // Mendeleev Communications. 2020. Vol. 30. No. 2. pp. 214-216.
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TY - JOUR
DO - 10.1016/j.mencom.2020.03.028
UR - https://mendcomm.colab.ws/publications/10.1016/j.mencom.2020.03.028
TI - Refolding of disulfide containing peptides in fusion with thioredoxin
T2 - Mendeleev Communications
AU - Logashina, Yulia A.
AU - Korolkova, Yuliya Vladimirovna
AU - Maleeva, Ekaterina Evgenievna
AU - Osmakov, Dmitry Igorevich
AU - Kozlov, Sergei Aleksandrovich
AU - Andreev, Yaroslav Alekseevich
PY - 2020
DA - 2020/03/02
PB - Mendeleev Communications
SP - 214-216
IS - 2
VL - 30
ER -
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@article{2020_Logashina,
author = {Yulia A. Logashina and Yuliya Vladimirovna Korolkova and Ekaterina Evgenievna Maleeva and Dmitry Igorevich Osmakov and Sergei Aleksandrovich Kozlov and Yaroslav Alekseevich Andreev},
title = {Refolding of disulfide containing peptides in fusion with thioredoxin},
journal = {Mendeleev Communications},
year = {2020},
volume = {30},
publisher = {Mendeleev Communications},
month = {Mar},
url = {https://mendcomm.colab.ws/publications/10.1016/j.mencom.2020.03.028},
number = {2},
pages = {214--216},
doi = {10.1016/j.mencom.2020.03.028}
}
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Logashina, Yulia A., et al. “Refolding of disulfide containing peptides in fusion with thioredoxin.” Mendeleev Communications, vol. 30, no. 2, Mar. 2020, pp. 214-216. https://mendcomm.colab.ws/publications/10.1016/j.mencom.2020.03.028.

Keywords

cysteine-rich peptides
peptide toxins
recombinant production
refolding
thioredoxin

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.

References

1.
Sea Anemones: Quiet Achievers in the Field of Peptide Toxins
J. Prentis P., Pavasovic A., S. Norton R.
Toxins, 2018
2.
Antimicrobial Peptides from Plants
Tam J., Wang S., Wong K., Tan W.
Pharmaceuticals, 2015
3.
Isolation, molecular cloning and antimicrobial activity of novel defensins from common chickweed (Stellaria media L.) seeds
Slavokhotova A.A., Odintsova T.I., Rogozhin E.A., Musolyamov A.K., Andreev Y.A., Grishin E.V., Egorov T.A.
Biochimie, 2011
4.
Production of disulfide-bonded proteins in Escherichia coli
Berkmen M.
Protein Expression and Purification, 2012
5.
Disulfide bond formation in prokaryotes: History, diversity and design
Hatahet F., Boyd D., Beckwith J.
Biochimica et Biophysica Acta - Proteins and Proteomics, 2014
6.
10.1016/j.mencom.2020.03.028_bib0030
Rosano
Front. Microbiol., 2014
8.
Increase of Solubility of Foreign Proteins in Escherichia coli by Coproduction of the Bacterial Thioredoxin (*)
Yasukawa T., Kanei-Ishii C., Maekawa T., Fujimoto J., Yamamoto T., Ishii S.
Journal of Biological Chemistry, 1995
9.
Fluorescent system based on bacterial expression of hybrid KcsA channels designed for Kv1.3 ligand screening and study
Kudryashova K.S., Nekrasova O.V., Kuzmenkov A.I., Vassilevski A.A., Ignatova A.A., Korolkova Y.V., Grishin E.V., Kirpichnikov M.P., Feofanov A.V.
Analytical and Bioanalytical Chemistry, 2013
10.
Novel mode of action of plant defense peptides - hevein-like antimicrobial peptides from wheat inhibit fungal metalloproteases
Slavokhotova A.A., Naumann T.A., Price N.P., Rogozhin E.A., Andreev Y.A., Vassilevski A.A., Odintsova T.I.
FEBS Journal, 2014
11.
Peptide from Sea Anemone Metridium senile Affects Transient Receptor Potential Ankyrin-repeat 1 (TRPA1) Function and Produces Analgesic Effect
Logashina Y.A., Mosharova I.V., Korolkova Y.V., Shelukhina I.V., Dyachenko I.A., Palikov V.A., Palikova Y.A., Murashev A.N., Kozlov S.A., Stensvåg K., Andreev Y.A.
Journal of Biological Chemistry, 2017
12.
Conversed mutagenesis of an inactive peptide to ASIC3 inhibitor for active sites determination
Osmakov D.I., Koshelev S.G., Andreev Y.A., Dyachenko I.A., Bondarenko D.A., Murashev A.N., Grishin E.V., Kozlov S.A.
Toxicon, 2016
13.
Optimizing Escherichia coli as a protein expression platform to produce Mycobacterium tuberculosis immunogenic proteins
Piubelli L., Campa M., Temporini C., Binda E., Mangione F., Amicosante M., Terreni M., Marinelli F., Pollegioni L.
Microbial Cell Factories, 2013
14.
Structure of Membrane-active Toxin from Crab Spider Heriaeus melloteei Suggests Parallel Evolution of Sodium Channel Gating Modifiers in Araneomorphae and Mygalomorphae
Berkut A.A., Peigneur S., Myshkin M.Y., Paramonov A.S., Lyukmanova E.N., Arseniev A.S., Grishin E.V., Tytgat J., Shenkarev Z.O., Vassilevski A.A.
Journal of Biological Chemistry, 2015
15.
Protein surface topography as a tool to enhance the selective activity of a potassium channel blocker
Berkut A.A., Chugunov A.O., Mineev K.S., Peigneur S., Tabakmakher V.M., Krylov N.A., Oparin P.B., Lihonosova A.F., Novikova E.V., Arseniev A.S., Grishin E.V., Tytgat J., Efremov R.G., Vassilevski A.A.
Journal of Biological Chemistry, 2019
16.
A fusion protein of conotoxin MVIIA and thioredoxin expressed in Escherichia coli has significant analgesic activity
Zhan J., Chen X., Wang C., Qiu J., Ma F., Wang K., Zheng S.
Biochemical and Biophysical Research Communications, 2003
17.
Spider toxins comprising disulfide-rich and linear amphipathic domains: a new class of molecules identified in the lynx spiderOxyopes takobius
Vassilevski A.A., Sachkova M.Y., Ignatova A.A., Kozlov S.A., Feofanov A.V., Grishin E.V.
FEBS Journal, 2013
18.
High Yield Production and Refolding of the Double-Knot Toxin, an Activator of TRPV1 Channels
Bae C., Kalia J., Song I., Yu J., Kim H.H., Swartz K.J., Kim J.I.
PLoS ONE, 2012
19.
Heterologous expression of barley and wheat oxalate oxidase in an E. coli trxB gor double mutant
Cassland P., Larsson S., Nilvebrant N., Jönsson L.J.
Journal of Biotechnology, 2004
20.
SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm
Lobstein J., Emrich C.A., Jeans C., Faulkner M., Riggs P., Berkmen M.
Microbial Cell Factories, 2012
21.
Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3
22.
Expression in Pichia pastoris and characterization of APETx2, a specific inhibitor of acid sensing ion channel 3
24.
A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid-sensitive channel in sensory neurons
Diochot S., Baron A., Rash L.D., Deval E., Escoubas P., Scarzello S., Salinas M., Lazdunski M.
EMBO Journal, 2004
25.
Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels
Chagot B., Escoubas P., Diochot S., Bernard C., Lazdunski M., Darbon H.
Protein Science, 2005
26.
New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties
Logashina Y.A., Solstad R.G., Mineev K.S., Korolkova Y.V., Mosharova I.V., Dyachenko I.A., Palikov V.A., Palikova Y.A., Murashev A.N., Arseniev A.S., Kozlov S.A., Stensvåg K., Haug T., Andreev Y.A.
Toxins, 2017
27.
Cyanogen bromide cleavage of proteins in salt and buffer solutions
Andreev Y.A., Kozlov S.A., Vassilevski A.A., Grishin E.V.
Analytical Biochemistry, 2010