Novel potential mechanism-based inhibitors of human leukocyte elastase and cathepsin G: derivatives of isothiazolidin-3-one.
A series of heterocyclic compounds designed to function as mechanism-based inhibitors of human leukocyte elastase and cathepsin G has been synthesized and their inhibitory activity was investigated. These isothiazolidin-3-one derivatives were found to be effective inhibitors of cathepsin G.
Groutas
W C
WC
Department of Chemistry, Wichita State University, KS 67260.
Chong
L S
LS
Venkataraman
R
R
D056649:Cathepsin G; D002403:Cathepsins / Q000037:antagonists & inhibitors* / Q000097:blood; D006801:Humans; D007700:Kinetics; D019272:Leukocyte Elastase; D007962:Leukocytes / Q000201:enzymology*; D015394:Molecular Structure; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D011480:Protease Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology*; D012697:Serine Endopeptidases; D013329:Structure-Activity Relationship; D013844:Thiazoles / Q000138:chemical synthesis / Q000494:pharmacology*
D011480:Protease Inhibitors; D013844:Thiazoles; D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D010196:Pancreatic Elastase; D019272:Leukocyte Elastase