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A phage display selected 7-mer peptide inhibitor of the Tannerella forsythia metalloprotease-like enzyme karilysin can be truncated to Ser-Trp-Phe-Pro

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A phage display selected 7-mer peptide inhibitor of the Tannerella forsythia metalloprotease-like enzyme karilysin can be truncated to Ser-Trp-Phe-Pro

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dc.contributor.author Skottrup, Peter Durand pl
dc.contributor.author Sørensen, Grete pl
dc.contributor.author Książek, Mirosław [SAP14019141] pl
dc.contributor.author Potempa, Jan [SAP11010833] pl
dc.contributor.author Riise, Erik pl
dc.date.accessioned 2016-05-20T06:00:02Z
dc.date.available 2016-05-20T06:00:02Z
dc.date.issued 2012 pl
dc.identifier.uri http://ruj.uj.edu.pl/xmlui/handle/item/26530
dc.language eng pl
dc.rights Udzielam licencji. Uznanie autorstwa 4.0 Międzynarodowa *
dc.rights.uri http://creativecommons.org/licenses/by/4.0/pl/legalcode *
dc.title A phage display selected 7-mer peptide inhibitor of the Tannerella forsythia metalloprotease-like enzyme karilysin can be truncated to Ser-Trp-Phe-Pro pl
dc.type JournalArticle pl
dc.abstract.en Tannerella forsythia is a gram-negative bacteria, which is strongly associated with the development of periodontal disease. Karilysin is a newly identified metalloprotease-like enzyme, that is secreted from T. forsythia. Karilysin modulates the host immune response and is therefore considered a likely drug target. In this study peptides were selected towards the catalytic domain from Karilysin (Kly18) by phage display. The peptides were linear with low micromolar binding affinities. The two best binders (peptide14 and peptide15), shared the consensus sequence XWFPXXXGGG. A peptide15 fusion with Maltose Binding protein (MBP) was produced with peptide15 fused to the N-terminus of MBP. The peptide15-MBP was expressed in E. coli and the purified fusion-protein was used to verify Kly18 specific binding. Chemically synthesised peptide15 (SWFPLRSGGG) could inhibit the enzymatic activity of both Kly18 and intact Karilysin (Kly48). Furthermore, peptide15 could slow down the autoprocessing of intact Kly48 to Kly18. The WFP motif was important for inhibition and a truncation study further demonstrated that the N-terminal serine was also essential for Kly18 inhibition. The SWFP peptide had a Ki value in the low micromolar range, which was similar to the intact peptide15. In conclusion SWFP is the first reported inhibitor of Karilysin and can be used as a valuable tool in structure-function studies of Karilysin. pl
dc.description.volume 7 pl
dc.description.number 10 pl
dc.identifier.doi 10.1371/journal.pone.0048537 pl
dc.identifier.eissn 1932-6203 pl
dc.title.journal PLoS ONE pl
dc.language.container eng pl
dc.affiliation Wydział Biochemii, Biofizyki i Biotechnologii : Zakład Mikrobiologii pl
dc.subtype Article pl
dc.identifier.articleid e48537 pl
dc.rights.original CC-BY; otwarte czasopismo; ostateczna wersja wydawcy; w momencie opublikowania; 0; pl
dc.identifier.project ROD UJ / P pl
.pointsMNiSW [2012 A]: 40


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Udzielam licencji. Uznanie autorstwa 4.0 Międzynarodowa Except where otherwise noted, this item's license is described as Udzielam licencji. Uznanie autorstwa 4.0 Międzynarodowa