Production of the recombinant antimicrobial peptide UBI18-35 in Escherichia coli; Protein Expression and Purification; Vol. 143

Bibliographic Details
Parent link:Protein Expression and Purification
Vol. 143.— 2018.— [P. 38-44]
Corporate Author: Национальный исследовательский Томский политехнический университет Исследовательская школа химических и биомедицинских технологий
Other Authors: Ashcheulova D. O., Efimova L. V. Lina Viktorovna, Lushchyk A. Y., Yantsevich A. V., Baykov A. N. Aleksandr Nikolaevich, Pershina A. G. Aleksandra Gennadievna
Summary:Title screen
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.
Language:English
Published: 2018
Subjects:
Online Access:https://doi.org/10.1016/j.pep.2017.10.011
Format: Electronic Book Chapter
KOHA link:https://koha.lib.tpu.ru/cgi-bin/koha/opac-detail.pl?biblionumber=667254
Description
Summary:Title screen
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.
DOI:10.1016/j.pep.2017.10.011