Production of the recombinant antimicrobial peptide UBI<sub>18-35</sub> in Escherichia coli

Abstract

Radiolabeled peptides derived from ubiquicidine (UBI) are of great interest for early and highly accurate scintigraphic detection and differentiation of infection and sterile inflammation. In the present work the recombinant antimicrobial peptide UBI_18-35 - a fragment of the human natural cationic peptide ubiquicidine - was produced in Escherichia coli for the first time. The insoluble expression of the peptide in fusion with ketosteroid isomerase provided high yield, about 6 mg of UBI_18-35 per liter. We developed an approach to produce the antimicrobial peptide UBI_18-35, that encompasses inclusion body isolation and size exclusion chromatography. This method could be the basis for industrial biotechnological production of diagnostic system components that are in high demand.

Original language	English
Pages (from-to)	38-44
Number of pages	7
Journal	Protein Expression and Purification
Volume	143
DOIs	https://doi.org/10.1016/j.pep.2017.10.011
Publication status	Published - 1 Mar 2018

Keywords

Antimicrobial peptides
Inclusion bodies
Ketosteroid isomerase
Size exclusion chromatography
Ubiquicidine

ASJC Scopus subject areas

Biotechnology

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10.1016/j.pep.2017.10.011

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Ashcheulova, D. O., Efimova, L. V., Lushchyk, A. Y., Yantsevich, A. V., Baikov, A. N., & Pershina, A. G. (2018). Production of the recombinant antimicrobial peptide UBI_18-35 in Escherichia coli. Protein Expression and Purification, 143, 38-44. https://doi.org/10.1016/j.pep.2017.10.011

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title = "Production of the recombinant antimicrobial peptide UBI18-35 in Escherichia coli",

abstract = "Radiolabeled peptides derived from ubiquicidine (UBI) are of great interest for early and highly accurate scintigraphic detection and differentiation of infection and sterile inflammation. In the present work the recombinant antimicrobial peptide UBI18-35 - a fragment of the human natural cationic peptide ubiquicidine - was produced in Escherichia coli for the first time. The insoluble expression of the peptide in fusion with ketosteroid isomerase provided high yield, about 6 mg of UBI18-35 per liter. We developed an approach to produce the antimicrobial peptide UBI18-35, that encompasses inclusion body isolation and size exclusion chromatography. This method could be the basis for industrial biotechnological production of diagnostic system components that are in high demand.",

keywords = "Antimicrobial peptides, Inclusion bodies, Ketosteroid isomerase, Size exclusion chromatography, Ubiquicidine",

author = "Ashcheulova, {Darya O.} and Efimova, {Lina V.} and Lushchyk, {Aliaksandr Ya} and Yantsevich, {Aliaksei V.} and Baikov, {Alexander N.} and Pershina, {Alexandra G.}",

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T1 - Production of the recombinant antimicrobial peptide UBI18-35 in Escherichia coli

AU - Ashcheulova, Darya O.

AU - Efimova, Lina V.

AU - Lushchyk, Aliaksandr Ya

AU - Yantsevich, Aliaksei V.

AU - Baikov, Alexander N.

AU - Pershina, Alexandra G.

PY - 2018/3/1

Y1 - 2018/3/1

N2 - Radiolabeled peptides derived from ubiquicidine (UBI) are of great interest for early and highly accurate scintigraphic detection and differentiation of infection and sterile inflammation. In the present work the recombinant antimicrobial peptide UBI18-35 - a fragment of the human natural cationic peptide ubiquicidine - was produced in Escherichia coli for the first time. The insoluble expression of the peptide in fusion with ketosteroid isomerase provided high yield, about 6 mg of UBI18-35 per liter. We developed an approach to produce the antimicrobial peptide UBI18-35, that encompasses inclusion body isolation and size exclusion chromatography. This method could be the basis for industrial biotechnological production of diagnostic system components that are in high demand.

AB - Radiolabeled peptides derived from ubiquicidine (UBI) are of great interest for early and highly accurate scintigraphic detection and differentiation of infection and sterile inflammation. In the present work the recombinant antimicrobial peptide UBI18-35 - a fragment of the human natural cationic peptide ubiquicidine - was produced in Escherichia coli for the first time. The insoluble expression of the peptide in fusion with ketosteroid isomerase provided high yield, about 6 mg of UBI18-35 per liter. We developed an approach to produce the antimicrobial peptide UBI18-35, that encompasses inclusion body isolation and size exclusion chromatography. This method could be the basis for industrial biotechnological production of diagnostic system components that are in high demand.

KW - Antimicrobial peptides

KW - Inclusion bodies

KW - Ketosteroid isomerase

KW - Size exclusion chromatography

KW - Ubiquicidine

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