a phage display selected 7-mer peptide inhibitor of the tannerella forsythia metalloprotease-like enzyme karilysin can be truncated to ser-trp-phe-pro噬菌体展示选择7-mer肽抑制剂的tannerella连翘metalloprotease-like酶karilysin ser-trp-phe-pro可以截断.pdfVIP

A Phage Display Selected 7-mer Peptide Inhibitor of the Tannerella forsythia Metalloprotease-Like Enzyme Karilysin Can Be Truncated to Ser-Trp-Phe-Pro 1 1 2 2,3 1 Peter Durand Skottrup *, Grete Sørensen , Miroslaw Ksiazek , Jan Potempa , Erik Riise 1 Biomolecular Interaction Group, Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark, 2 Department of Microbiology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Krakow, Poland, 3 Oral Health and Systemic Diseases Research Group, University of Louisville, School of Dentistry, Louisville, Kentucky, United States of America Abstract 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