| http://purl.uniprot.org/citations/15625724 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15625724 | http://www.w3.org/2000/01/rdf-schema#comment | "Human beta-defensins comprise a large number of peptides that play a functional role in the innate and adaptive immune system. Recently, clusters of new beta-defensin genes with predominant expression in testicular tissue have been discovered on different chromosomes by bioinformatics. beta-Defensins share a common pattern of three disulfides that are essential for their biological effects. Here we report for the first time the chemical synthesis of the new fully disulfide-bonded beta-defensins hBD-27 and hBD-28, and compare the results with synthetic procedures to obtain the known hBD-2 and hBD-3. While hBD-27 was readily converted into a product with the desired disulfide pattern by oxidative folding, hBD-28 required a selective protective group strategy to introduce the three disulfide bonds. The established synthetic processes were applied to the synthesis of hBD-2, which, like hBD-27, was accessible by oxidative folding, whereas hBD-3 required a selective strategy comparable to hBD-28. Experimental work demonstrated that trityl, acetamidomethyl, and t-butyl are superior to other protection strategies. However, the suitable pairwise arrangement of the protective groups can be different, as shown here for hBD-3 and hBD-28. Determination of the minimum inhibitory concentration against different bacteria revealed that hBD-27, in contrast to other beta-defensins tested, has virtually no antimicrobial activity. Compared to the other peptides tested, hBD-27 showed almost no cytotoxic activity, measured by hemoglobin release of erythrocytes. This might be due to the low positive net charge, which is significantly higher for hBD-2, hBD-3, and hBD-28."xsd:string |
| http://purl.uniprot.org/citations/15625724 | http://purl.org/dc/terms/identifier | "doi:10.1002/bip.20193"xsd:string |
| http://purl.uniprot.org/citations/15625724 | http://purl.uniprot.org/core/author | "Schulz A."xsd:string |
| http://purl.uniprot.org/citations/15625724 | http://purl.uniprot.org/core/author | "Adermann K."xsd:string |
| http://purl.uniprot.org/citations/15625724 | http://purl.uniprot.org/core/author | "Schulz-Maronde S."xsd:string |
| http://purl.uniprot.org/citations/15625724 | http://purl.uniprot.org/core/author | "Kluver E."xsd:string |
| http://purl.uniprot.org/citations/15625724 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15625724 | http://purl.uniprot.org/core/name | "Biopolymers"xsd:string |
| http://purl.uniprot.org/citations/15625724 | http://purl.uniprot.org/core/pages | "34-49"xsd:string |
| http://purl.uniprot.org/citations/15625724 | http://purl.uniprot.org/core/title | "Engineering disulfide bonds of the novel human beta-defensins hBD-27 and hBD-28: differences in disulfide formation and biological activity among human beta-defensins."xsd:string |
| http://purl.uniprot.org/citations/15625724 | http://purl.uniprot.org/core/volume | "80"xsd:string |
| http://purl.uniprot.org/citations/15625724 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15625724 |
| http://purl.uniprot.org/citations/15625724 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15625724 |
| http://purl.uniprot.org/uniprot/Q7Z7B8#attribution-4709CBBBB29F223762101987DAC99B34 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15625724 |
| http://purl.uniprot.org/uniprot/O15263#attribution-4709CBBBB29F223762101987DAC99B34 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15625724 |
| http://purl.uniprot.org/uniprot/P81534#attribution-4709CBBBB29F223762101987DAC99B34 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15625724 |