کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1375917 | 981947 | 2009 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Modification of the N-terminal sulfonyl residue in 3-amidinophenylalanine-based matriptase inhibitors
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Replacement of the N-terminal β-alanyl-amide moiety in previously identified matriptase inhibitors by non-charged aryl groups caused a slightly decreased potency and partially reduced selectivity, especially towards thrombin. However, some of these analogues are still potent matriptase inhibitors with Ki-values <10 nM. In contrast, improved activity was observed for newly designed tribasic analogues, especially for compound 21, which inhibits matriptase with an Ki-value of 80 pM.
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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 19, Issue 1, 1 January 2009, Pages 67–73
Journal: Bioorganic & Medicinal Chemistry Letters - Volume 19, Issue 1, 1 January 2009, Pages 67–73
نویسندگان
Torsten Steinmetzer, Daniel Dönnecke, Martin Korsonewski, Claudia Neuwirth, Peter Steinmetzer, Alexander Schulze, Sebastian Martin Saupe, Andrea Schweinitz,