TY  - JOUR
AB  - 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.
AU  - Moran, BW
AU  - Anderson, FP
AU  - Ruth, DM
AU  - Fágáin, CO
AU  - Dalton, JP
AU  - Kenny, PTM
DA  - 2010/02/01
DO  - 10.3109/14756360902888184
EP  - 12
JO  - Journal of Enzyme Inhibition and Medicinal Chemistry
PY  - 2010/02/01
SP  - 1
TI  - Fluorobenzoyl dipeptidyl derivatives as inhibitors of the Fasciola hepatica cysteine protease cathepsin L1
VL  - 25
Y1  - 2010/02/01
Y2  - 2026/05/19
ER  -