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. 2018 Mar:143:38-44.
doi: 10.1016/j.pep.2017.10.011. Epub 2017 Oct 21.

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

Darya O Ashcheulova  1 , Lina V Efimova  2 , Aliaksandr Ya Lushchyk  3 , Aliaksei V Yantsevich  3 , Alexander N Baikov  2 , Alexandra G Pershina  4
Affiliations

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

Darya O Ashcheulova et al. Protein Expr Purif. 2018 Mar.

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.

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