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Proteolytic Degradation of reduced Human Beta Defensin 1 generates a Novel Antibiotic Octapeptide
Dr. Margarete FischerBosch-Institute of Clinical Pharmacology, Stuttgart and University of Tuebingen, Tuebingen, Germany; Present address: Wallenberg Laboratory, University of Gothenburg, Gothenburg, Sweden.ORCID iD: 0000-0002-6716-8284
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2019 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 9, article id 3640Article in journal (Refereed) Published
Abstract [en]

Microbial resistance against clinical used antibiotics is on the rise. Accordingly, there is a high demand for new innovative antimicrobial strategies. The host-defense peptide human beta-defensin 1 (hBD-1) is produced continuously by epithelial cells and exhibits compelling antimicrobial activity after reduction of its disulphide bridges. Here we report that proteolysis of reduced hBD-1 by gastrointestinal proteases as well as human duodenal secretions produces an eight-amino acid carboxy-terminal fragment. The generated octapeptide retains antibiotic activity, yet with distinct characteristics differing from the full-length peptide. We modified the octapeptide by stabilizing its termini and by using non-natural D-amino acids. The native and modified peptide variants showed antibiotic activity against pathogenic as well as antibiotic-resistant microorganisms, including E. coli, P. aeruginosa and C. albicans. Moreover, in an in vitro C. albicans infection model the tested peptides demonstrated effective amelioration of C. albicans infection without showing cytotoxity on human cells. In summary, protease degradation of hBD-1 provides a yet unknown mechanism to broaden antimicrobial host defense, which could be used to develop defensin-derived therapeutic applications.

Place, publisher, year, edition, pages
Nature Publishing Group, 2019. Vol. 9, article id 3640
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Immunology
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URN: urn:nbn:se:umu:diva-166015DOI: 10.1038/s41598-019-40216-2ISI: 000460391500023PubMedID: 30842543OAI: oai:DiVA.org:umu-166015DiVA, id: diva2:1376361
Available from: 2019-12-09 Created: 2019-12-09 Last updated: 2019-12-11Bibliographically approved

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