Abstract
The P2-P3 amide of dipeptide cathepsin K inhibitors can be replaced by the metabolically stable trifluoroethylamine group. The non-basic nature of the nitrogen allows the important hydrogen bond to Gly66 to be made. The resulting compounds are 10- to 20-fold more potent than the corresponding amide derivatives. Compound 8 is a 5 pM inhibitor of human cathepsin K with >10,000-fold selectivity over other cathepsins.
MeSH terms
-
Amides / chemistry
-
Cathepsin K
-
Cathepsins / antagonists & inhibitors*
-
Dipeptides / chemical synthesis
-
Dipeptides / pharmacology
-
Ethylamines / chemical synthesis
-
Ethylamines / pharmacology*
-
Humans
-
Hydrogen Bonding
-
Inhibitory Concentration 50
-
Protease Inhibitors / chemical synthesis*
-
Protease Inhibitors / pharmacology
-
Structure-Activity Relationship
Substances
-
Amides
-
Dipeptides
-
Ethylamines
-
Protease Inhibitors
-
trifluoroethylamine
-
Cathepsins
-
CTSK protein, human
-
Cathepsin K