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FEBS Lett. 2006 Apr 17;580(9):2227-32. Epub 2006 Mar 20.

Inhibition of human matriptase by eglin c variants.

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1
Department of Pharmacology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, Que., Canada J1H 5N4.

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, R(1)K(4)'-eglin, which had the wild-type Pro(45) (P1 position) and Tyr(49) (P4' position) residues replaced with Arg and Lys, respectively, led to the production of a selective, high affinity (K(i) 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 family.

PMID:
16566926
DOI:
10.1016/j.febslet.2006.03.030
[Indexed for MEDLINE]
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