Inhibition of human matriptase by eglin c variants
- 20 March 2006
- journal article
- Published by Wiley in FEBS Letters
- Vol. 580 (9) , 2227-2232
- https://doi.org/10.1016/j.febslet.2006.03.030
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 4nM) 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 familyKeywords
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