| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1364983 | Bioorganic & Medicinal Chemistry Letters | 2008 | 4 Pages |
Abstract
Nonpeptidic, selective, and potent cathepsin S inhibitors were derived from an in-house pyrrolopyrimidine cathepsin K inhibitor by modification of the P2 and P3 moieties. The pyrrolopyrimidine-based inhibitors show nanomolar inhibition of cathepsin S with over 100-fold selectivity against other cysteine proteases, including cathepsin K and L. Some of the inhibitors showed cellular activities in mouse splenocytes as well as oral bioavailabilities in rats.
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Related Topics
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Authors
Osamu Irie, Takeru Ehara, Atsuko Iwasaki, Fumiaki Yokokawa, Junichi Sakaki, Hajime Hirao, Takanori Kanazawa, Naoki Teno, Miyuki Horiuchi, Ichiro Umemura, Hiroki Gunji, Keiichi Masuya, Yuko Hitomi, Genji Iwasaki, Kazuhiko Nonomura, Keiko Tanabe,