کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2052925 1074245 2006 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Inhibition of human matriptase by eglin c variants
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Inhibition of human matriptase by eglin c variants
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 580, Issue 9, 17 April 2006, Pages 2227–2232
نویسندگان
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