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.
| Original language | English |
|---|---|
| Pages (from-to) | 38-44 |
| Number of pages | 7 |
| Journal | Protein Expression and Purification |
| Volume | 143 |
| DOIs | |
| Publication status | Published - 1 Mar 2018 |
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Keywords
- Antimicrobial peptides
- Inclusion bodies
- Ketosteroid isomerase
- Size exclusion chromatography
- Ubiquicidine
ASJC Scopus subject areas
- Biotechnology
Cite this
Production of the recombinant antimicrobial peptide UBI18-35 in Escherichia coli. / Ashcheulova, Darya O.; Efimova, Lina V.; Lushchyk, Aliaksandr Ya; Yantsevich, Aliaksei V.; Baikov, Alexander N.; Pershina, Alexandra G.
In: Protein Expression and Purification, Vol. 143, 01.03.2018, p. 38-44.Research output: Contribution to journal › Article
}
TY - JOUR
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
UR - http://www.scopus.com/inward/record.url?scp=85032341472&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85032341472&partnerID=8YFLogxK
U2 - 10.1016/j.pep.2017.10.011
DO - 10.1016/j.pep.2017.10.011
M3 - Article
VL - 143
SP - 38
EP - 44
JO - Protein Expression and Purification
JF - Protein Expression and Purification
SN - 1046-5928
ER -