Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052925 | FEBS Letters | 2006 | 6 Pages |
Abstract
Based on the enzyme specificity of matriptase, a type II transmembrane serine protease (TTSP) overexpressed in epithelial tumors, we screened a cDNA library expressing variants of the protease inhibitor eglin c in order to identify potent matriptase inhibitors. The most potent of these, R1K4′-eglin, which had the wild-type Pro45 (P1 position) and Tyr49 (P4′ position) residues replaced with Arg and Lys, respectively, led to the production of a selective, high affinity (Ki of 4 nM) and proteolytically stable inhibitor of matriptase. Screening for eglin c variants could yield specific, potent and stable inhibitors to matriptase and to other members of the TTSP family.
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Authors
Antoine Désilets, Jean-Michel Longpré, Marie-Ève Beaulieu, Richard Leduc,