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Bioorg Med Chem Lett. 2004 Jun 21;14(12):3043-7.

A novel series of potent and selective small molecule inhibitors of the complement component C1s.

Author information

1
3-Dimensional Pharmaceuticals Inc, 665 Stockton Drive, Exton, PA 19341, USA. nsubasin@prdus.jnj.com

Abstract

Activation of the classical pathway of complement has been implicated in disease states such as hereditary angioedema, ischemia-reperfusion injury and acute transplant rejection. The trypsin-like serine protease C1s represents a pivotal upstream point of control in the classical pathway of complement activation and is therefore likely to be a useful target in the therapeutic intervention of these disease states. A series of thiopheneamidine-based inhibitors of C1s has been optimized to give a 70 nM inhibitor that inhibits the classical pathway of complement activation in vitro.

PMID:
15149641
DOI:
10.1016/j.bmcl.2004.04.034
[Indexed for MEDLINE]

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