Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1374952 | Bioorganic & Medicinal Chemistry Letters | 2006 | 5 Pages |
Abstract
Inhibiting the classical pathway of complement activation by attenuating the proteolytic activity of the serine protease C1s is a potential strategy for the therapeutic intervention in disease states such as hereditary angioedema, ischemia–reperfusion injury, and acute transplant rejection. A series of arylsulfonylthiophene-2-carboxamidine inhibitors of C1s were synthesized and evaluated for C1s inhibitory activity. The most potent compound had a Ki of 10 nM and >1000-fold selectivity over uPA, tPA, FXa, thrombin, and plasmin.
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Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Nalin L. Subasinghe, Jeremy M. Travins, Farah Ali, Hui Huang, Shelley K. Ballentine, Juan José Marugán, Ehab Khalil, Heather R. Hufnagel, Roger F. Bone, Renee L. DesJarlais, Carl S. Crysler, Nisha Ninan, Maxwell D. Cummings, Christopher J. Molloy,