@article{ref1,
title="[Synthetic inhibitors targeting serine and aspartic acid proteases]",
journal="Journal de Pharmacie de Belgique",
year="1996",
author="Reboud-Ravaux, M. C. and Boggetto, N. D. and Doucet, C. E. and de Rosny, E. H. and Vergely, I. B. and Thierry, N. M. and Amour, A. J.",
volume="51",
number="3",
pages="161-164",
abstract="The interaction of novel series of synthetic inhibitors with various serine proteases (leukocyte elastase, thrombin, cathepsin G, chymotrypsin, plasminogen activators and plasmin) and an aspartic protease (HIV-1 protease) were studied. Various aspects were analyzed: mechanism of action, structure-activity relationships, and in some cases, molecular modelling and biological evaluation. Functionalized cyclopeptides and N-aryl azetidin-2-ones behaved as suicide substrates acting specifically on trypsin-like proteases (thrombin or urokinase) and elastases, respectively. Novel hydrazinopeptides acted as reversible inhibitors of elastases. Coumarin derivatives inactivated very efficiently chymotrypsin-like proteases (k(inact)/K(I) = 760,000 M(-1).s(-1)). Inhibitors of HIV-1 protease acting either as inactivators or dimerization inhibitors are under investigation. The inhibitors described above are useful for elucidating the biological roles of the target enzymes and constitute potential drugs.<p /><p>Language: fr</p>",
language="fr",
issn="0047-2166",
doi="",
url="http://dx.doi.org/"
}