173253-46-8Relevant academic research and scientific papers
Structure-based design of nonpeptide inhibitors of interleukin-1β converting enzyme (ICE, Caspase-1)
Shahripour, Aurash B,Plummer, Mark S,Lunney, Elizabeth A,Albrecht, Hans P,Hays, Sheryl J,Kostlan, Catherine R,Sawyer, Tomi K,Walker, Nigel P.C,Brady, Kenneth D,Allen, Hamish J,Talanian, Robert V,Wong, Winnie W,Humblet, Christine
, p. 31 - 40 (2007/10/03)
A novel class of reversible inhibitors of Interleukin-1β-converting enzyme (ICE, caspase-1) were discovered by iterative structure-based design. Guided by the X-ray crystal structure of analogues 1, 7 and 10 bound to ICE, we have designed a non-peptide series of small molecule inhibitors. These compounds incorporate an arylsulfonamide moiety which replaces Val-His unit (P3-P2 residues) amino acids of the native substrate. The synthesis of the core structure, structure-activity relationships (SARs), and proposed binding orientation based on molecular modeling studies for this serie of ICE inhibitors are described. Copyright
N-heterocyclyl sulphonamide derivatives and their use as endothelin antagonists
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, (2008/06/13)
The invention concerns pharmaceutically useful N-heterocyclyl sulphonamide derivatives, their pharmaceutically acceptable salts, processes for their manufacture, their use for antagonising one or more actions of endothelin in a human or other warm-blooded animal, their use in methods of treatment of diseases or medical conditions in which elevated or abnormal levels of endothelin play a significant causative role.
