{ "labelLang" : "hun", "responseDate" : "2024-03-29 16:09", "content" : { "otype" : "JournalArticle", "mtid" : 30773618, "status" : "APPROVED", "published" : true, "comment" : "Department of Internal Medicine 1, University Hospital Tuebingen, Tuebingen, Germany \n Dr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology, Stuttgart and University of Tuebingen, Tuebingen, Germany \n Institute of Immunology, Vetsuisse Faculty, University of Zürich, Zurich, Switzerland \n Institute of Dermatology, University Hospital Tuebingen, Tuebingen, Germany \n Institute of Medical Microbiology and Hygiene, University Hospital Tuebingen, Tuebingen, Germany \n Wallenberg Laboratory, University of Gothenburg, Gothenburg, Sweden \n Institute of Immunology, Vetsuisse Faculty, University of Zürich, Zurich, Switzerland \n Export Date: 27 August 2019 \n Correspondence Address: Wehkamp, J.; Department of Internal Medicine 1, University Hospital TuebingenGermany; email: jan.wehkamp@med.uni-tuebingen.de \n Funding text 1: We thank Marion Strauß for excellent technical assistance and Birgit Fehrenbacher, Renate Nordin and Theresia Schneider (University Hospital Tuebingen, Department of Dermatology) for performing electron microscopic analyses. This work was supported by Deutsche Forschungsgemenischaft (DFG) and Heisenberg Professorship (JW).\nDepartment of Internal Medicine 1, University Hospital Tuebingen, Tuebingen, Germany \n Dr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology, Stuttgart and University of Tuebingen, Tuebingen, Germany \n Institute of Immunology, Vetsuisse Faculty, University of Zürich, Zurich, Switzerland \n Institute of Dermatology, University Hospital Tuebingen, Tuebingen, Germany \n Institute of Medical Microbiology and Hygiene, University Hospital Tuebingen, Tuebingen, Germany \n Wallenberg Laboratory, University of Gothenburg, Gothenburg, Sweden \n Institute of Immunology, Vetsuisse Faculty, University of Zürich, Zurich, Switzerland \n Cited By :4 \n Export Date: 24 August 2020 \n Correspondence Address: Wehkamp, J.; Department of Internal Medicine 1, University Hospital TuebingenGermany; email: jan.wehkamp@med.uni-tuebingen.de\nExport Date: 16 July 2021", "unhandledTickets" : 0, "deleted" 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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. 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