177218-76-7Relevant academic research and scientific papers
Potent carboxylate inhibitors of stromelysin containing P2' piperazic acids and P1' biaryl moeities
Cherney, Robert J.,Decicco, Carl P.,Nelson, David J.,Wang, Li,Meyer, Dayton T.,Hardman, Karl D.,Copeland, Robert A.,Arner, Elizabeth C.
, p. 1757 - 1762 (2007/10/03)
Several carboxylate derivatives with variation at the P1' residue were synthesized and evaluated as stromelysin (MMP-3) inhibitors. Compounds containing a bipbenyl moiety at P1' were found to be potent inhibitors of MMP-3. An X-ray crystal structure of the most potent compound, carboxylate 19, revealed an important interaction between the inhibitor's biphenyl and histidine 224 in the S1' pocket of MMP-3.
Orally active inhibitors of stromelysin-1 (MMP-3)
Chapman, Kevin T.,Durette, Philippe L.,Caldwell, Charles G.,Sperow, Kelly M.,Niedzwiecki, Lisa M.,Harrison, Richard K.,Saphos, Cheryl,Christen, Amy J.,Olszewski, Julie M.,Moore, Vernon L.,MacCoss, Malcolm,Hagmann, William K.
, p. 803 - 806 (2007/10/03)
Further development of N-carboxyalkyl dipeptide inhibitors of stromelysin-1 (MMP-3) led to the discovery of C-carboxyalkyl dipeptide analogs with improved oral bioavailability. An in vivo assay of human MMP-3 mediated degradation of a macromolecular substrate in an extravascular space is described and inhibition studies are reported.
