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Journals Bioorganic and Medicinal Chemistry Volume 16 Issue 18

1 <h5>Introduction</h5> Matrix metalloproteinases (MMPs) belong to the M 10 clan of zinc containing endopeptidases that have been shown to play an important role in a variety of physiological functions. 1 Their activity is controlled by endogenous inhibitors, mainly tissue inhibitors of metalloproteinases (TIMP). Disruption of the finely tuned MMPs/TIMPs balance is observed in several pathologies including osteoarthritis, atherosclerosis, aneurysm, pulmonary emphysema, neurodegenerative diseases, and cancer. Consequently, the development of synthetic MMP inhibitors (MMPIs) possessing a high potency and selectivity has attracted significant efforts aiming to interfere with the progression of these pathologies. 2 To date a myriad of broad spectrum MMP inhibitors has been synthesized but the results of the first clinical trials, notably in cancer area, proved to be rather disappointing due to the multifaceted functions of this endopeptidase family. 3 Indeed, besides acting as matrix degrading enzymes, MMPs can hydrolyze or activate cytokines and growth factors, shed or activate receptors, and modulate the control of proteinases from other families through proteolysis of proteinase inhibitors. Important side effects and lack of selectivity owing to similarities of the active sites of other metalloproteinases (ACE, ADAM, ADAMT) were also reported to be responsible for the inefficiency of early

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Introduction of the 4-(4-bromophenyl)benzenesulfonyl group to hydrazide analogs of Ilomastat leads to potent gelatinase B (MMP-9) inhibitors with improved selectivity

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  • Publisher Elsevier
  • Copyright Copyright © 2008 Elsevier Ltd
  • ISSN 0968-0896
  • D.O.I. 10.1016/j.bmc.2008.07.041
  • Publisher site Get PDF  

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