@article{ref1,
title="Inhibition of human leukocyte elastase by functionalized N-aryl azetidin-2-ones: substituent effects at C-3 and benzylic positions",
journal="European journal of medicinal chemistry",
year="1995",
author="Vergely, I. and Boggetto, N. and Okochi, V. and Golpayegani, S. and Reboud-Ravaux, M. and Kobaiter, R. and Joyeau, R. and Wakselman, M.",
volume="30",
number="3",
pages="199-208",
abstract="A series of functionalized N-aryl azetidin-2-ones with a latent alkylating group was prepared by a flexible four-step synthesis. They met criteria expected for a suicide-type inactivation of human leukocyte elastase (HLE) and porcine pancreatic elastase (PPE), with no inactivation of trypsin- and chymotrypsin-like proteases. The inhibition potency was dependent on the halogen substituents at C-3 (F, F; Cl, Cl; Br, Br) and the nature and the position relative to nitrogen of the latent benzylic leaving group (F, Cl, Br). Better inactivations of HLE compared with PPE were observed with azetidinones gem-disubstituted by Cl and Br rather than by F. Their protio analogs, which are devoid of the latent quinoniminium methide electrophile, behave as simple substrates of elastases. © 1995 Elsevier, Paris.<p /><p>Language: en</p>",
language="en",
issn="0223-5234",
doi="10.1016/0223-5234(96)88226-2",
url="http://dx.doi.org/10.1016/0223-5234(96)88226-2"
}