Fluorobenzoyl dipeptidyl derivatives as inhibitors of the Fasciola hepatica cysteine protease cathepsin L1
- Publication Type:
- Journal Article
- Citation:
- Journal of Enzyme Inhibition and Medicinal Chemistry, 2010, 25 (1), pp. 1 - 12
- Issue Date:
- 2010-02-01
Closed Access
| Filename | Description | Size | |||
|---|---|---|---|---|---|
 | 2010002603OK.pdf | 883.36 kB |
Copyright Clearance Process
- Recently Added
- In Progress
- Closed Access
This item is closed access and not available.
Cathepsins are known to have many important physiological roles and provide a viable target for inhibition. Fluorobenzoyl dipeptide derivatives were synthesized and tested for biological activity in an effort to find an efficient inhibitor of the cysteine protease cathepsin L. Thirty-six novel inhibitors (1-36) were synthesized from protected amino acids via the standard DCC/HOBt coupling protocol, containing a benzyl ester or a nitrile as an electrophilic warhead. The activity of the inhibitors was evaluated against cathepsin L and IC50 values calculated. Modification of both amino acids and terminal groups afforded compounds with single digit micromolar inhibition. Results utilizing the benzoyl-L-leucine-glycine nitrile backbone are comparable to that for the commercially available inhibitor 39. © 2010 Informa UK Ltd.
Please use this identifier to cite or link to this item: