Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1378503 | Bioorganic & Medicinal Chemistry Letters | 2005 | 5 Pages |
Abstract
Several novel ketoamide-based inhibitors of cathepsin K have been identified. Starting from a modestly potent inhibitor, structural screening of P2 elements led to 100-fold enhancements in inhibitory activity. Modifications to one of these leads resulted in an orally bioavailable cathepsin K inhibitor.
Graphical abstractSeveral novel ketoamide-based inhibitors of cathepsin K have been identified. Starting from a modestly potent inhibitor, structural screening of P2 elements led to 100-fold enhancements in inhibitory activity. Modifications to one of these leads resulted in an orally bioavailable cathepsin K inhibitor.Figure optionsDownload full-size imageDownload as PowerPoint slide
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
David G. Barrett, John G. Catalano, David N. Deaton, Stacey T. Long, Robert B. McFadyen, Aaron B. Miller, Larry R. Miller, Kevin J. Wells-Knecht, Lois L. Wright,