TY - JOUR
T1 - Development of peptidyl α-keto-β-aldehydes as new inhibitors of cathepsin L - Comparisons of potency and selectivity profiles with cathepsin B
AU - Lynas, J.F.
AU - Hawthorne, S.J.
AU - Walker, B.
N1 - cited By 18
PY - 2000
Y1 - 2000
N2 - We have utilized previously known substrate and inhibitor specificity profiles for the lysosomal cysteine protease, cathepsin L, to design a new series of putative inhibitors of this enzyme, based on di- and tri-peptidyl α-keto-β-aldehydes. Kinetic evaluation of these compounds revealed Z-Phe-Tyr(OBut)-COCHO, with a Ki=0.6 nM, to be the most potent, synthetic reversible inhibitor of cathepsin L reported to date
AB - We have utilized previously known substrate and inhibitor specificity profiles for the lysosomal cysteine protease, cathepsin L, to design a new series of putative inhibitors of this enzyme, based on di- and tri-peptidyl α-keto-β-aldehydes. Kinetic evaluation of these compounds revealed Z-Phe-Tyr(OBut)-COCHO, with a Ki=0.6 nM, to be the most potent, synthetic reversible inhibitor of cathepsin L reported to date
U2 - 10.1016/S0960-894X(00)00340-1
DO - 10.1016/S0960-894X(00)00340-1
M3 - Article
VL - 10
SP - 1771
EP - 1773
JO - Bioorganic and Medicinal Chemistry Letters
JF - Bioorganic and Medicinal Chemistry Letters
IS - 15
ER -