Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1375917 | Bioorganic & Medicinal Chemistry Letters | 2009 | 7 Pages |
Abstract
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.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Torsten Steinmetzer, Daniel Dönnecke, Martin Korsonewski, Claudia Neuwirth, Peter Steinmetzer, Alexander Schulze, Sebastian Martin Saupe, Andrea Schweinitz,