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Bioorg. Med. Chem. Lett. · May 2013
Identification of new peptide amides as selective cathepsin L inhibitors: the first step towards selective irreversible inhibitors?
- Ana Torkar, Brigita Lenarčič, Tamara Lah, Vincent Dive, and Laurent Devel.
- Department of Genetic Toxicology and Cancer Biology, National Institute of Biology, Večna pot 111, 1000 Ljubljana, Slovenia.
- Bioorg. Med. Chem. Lett. 2013 May 15; 23 (10): 2968-73.
AbstractA small library of peptide amides was designed to profile the cathepsin L active site. Within the cathepsin family of cysteine proteases, the first round of selection was on cathepsin L and cathepsin B, and then selected hits were further evaluated for binding to cathepsin K and cathepsin S. Five highly selective sequences with submicromolar affinities towards cathepsin L were identified. An acyloxymethyl ketone warhead was then attached to these sequences. Although these original irreversible inhibitors inactivate cathepsin L, it appears that the nature of the warhead drastically impact the selectivity profile of the resulting covalent inhibitors.Copyright © 2013 Elsevier Ltd. All rights reserved.
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