| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1374731 | Bioorganic & Medicinal Chemistry Letters | 2006 | 5 Pages |
Abstract
A series of ketopiperazine-based renin inhibitors designed to interact in the S3 sub-pocket of the renin protein were evaluated for renin inhibitory activity. The investigation revealed that linear and sterically small side chain substituents are preferred in the S3 sub-pocket for optimal renin inhibition. Polar groups in the S3 sub-pocket were not well tolerated and caused a reduction in renin inhibitory activity. Further, compounds with c log P's ⩽ 3 demonstrated a dramatic reduction in CYP3A4 inhibitory activity.
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Authors
Daniel D. Holsworth, Cuiman Cai, Xue-Min Cheng, Wayne L. Cody, Dennis M. Downing, Noe Erasga, Chitase Lee, Noel A. Powell, Jeremy J. Edmunds, Michael Stier, Mehran Jalaie, Erli Zhang, Pat McConnell, Michael J. Ryan, John Bryant, Tingsheng Li,