Abstract: A series of peptidyl N-nitrosoanilines were designed, synthesized, and evaluated as inactivators of cysteine protease papain. These new compounds exhibited different inhibitory activities toward cysteine protease papain in a time- and concentration-dependent manner with second-order rate constants (ki/KI) ranging over two orders of magnitude from 0.604 M-1 sec-1 (1) to 100.36 M-1 sec-1 (7). Formation of the S-NO bond in papain is corroborated by evidence obtained from spectroscopic analyses. The fact that S-nitrosylated enzyme can regain its activity upon addition of thiol compounds such as glutathione makes this class of compounds suitable as templates for the development of potent reversible and covalent cysteine protease inhibitors.
Publication Year: 1999
Publication Date: 1999-01-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
Access and Citation
Cited By Count: 3
AI Researcher Chatbot
Get quick answers to your questions about the article from our AI researcher chatbot