Generic placeholder image

Current Topics in Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 1568-0266
ISSN (Online): 1873-4294

Peptidyl Fluoro-Ketones as Proteolytic Enzyme Inhibitors

Author(s): Monica Sani, Roberta Sinisi and Fiorenza Viani

Volume 6, Issue 14, 2006

Page: [1545 - 1566] Pages: 22

DOI: 10.2174/156802606777951064

Price: $65

conference banner
Abstract

Proteolytic enzymes are involved in many important physiological processes. Because of the critical roles played by these enzymes, aberrations in regulation of their activities can lead to pathological conditions. For this reason, finding inhibitors selective for a proteolytic enzyme that is contributing to a medical problem can be an effective therapeutic strategy. The introduction of fluorine in the backbone of proteolytic enzyme substrates can lead to active and selective inhibitors belonging to the peptidyl fluorinated ketone family. Fluorine not only can influence the mechanism of substrate/enzyme recognition events but also can modify the in vivo profile of the substrate. Although prediction of the total effects of fluorine on the pharmacokinetic parameters can be difficult, the pharmaceutical interest in the synthesis and biological evaluation of peptidyl fluorinated ketones highlights the potential of this family of molecules as therapeutically useful inhibitors.

Keywords: Activated ketone-based inhibitors, Aspartic proteases, Plasmepsin, Human Leucocyte Elastase (HLE), Chymotrypsin inhibitor, Thrombin

« Previous

Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy