| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1368551 | Bioorganic & Medicinal Chemistry Letters | 2016 | 5 Pages |
Abstract
The serine protease matriptase-2 has attracted much attention as a potential target for the treatment of iron overload diseases. In this study, a series of 27 symmetric, achiral bisbenzamidines was evaluated for inhibitory activity against human matriptase-2, against the closely related enzyme human matriptase, as well as against human thrombin, bovine factor Xa and human trypsin. The conformationally restricted piperazine derivative 19 and the oxamide-derived bisbenzamidine 1 were identified as the most potent inhibitors of this series for matriptase-2 and matriptase, respectively.
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Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Anna-Madeleine Beckmann, Erik Gilberg, Susanne Gattner, Tien L. Huang, Jean Jacques Vanden Eynde, Annie Mayence, Jürgen Bajorath, Marit Stirnberg, Michael Gütschow,