AI Article Synopsis
- Radiolabeled peptides from ubiquicidine (UBI) are promising for accurately detecting infections and differentiating them from sterile inflammation.
- Researchers successfully produced the antimicrobial peptide UBI in Escherichia coli, achieving a high yield of about 6 mg per liter.
- The developed method involves isolating inclusion bodies and using size exclusion chromatography, potentially paving the way for industrial production of these diagnostic components.
Article 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 - 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 per liter. We developed an approach to produce the antimicrobial peptide UBI, 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.
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| http://dx.doi.org/10.1016/j.pep.2017.10.011 | DOI Listing |
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