Synthesis and evaluation of chloromethyl sulfoxides as a new class of selective irreversible cysteine protease inhibitors
AJ Brouwer, A Bunschoten, RMJ Liskamp
Index: Brouwer, Arwin J.; Bunschoten, Anton; Liskamp, Rob M.J. Bioorganic and Medicinal Chemistry, 2007 , vol. 15, # 22 p. 6985 - 6993
Full Text: HTML
Citation Number: 2
Abstract
The synthesis and biological evaluation of a new class of selective irreversible cysteine protease inhibitors is described. A set of amino acid based chloromethyl sulfoxides was prepared and they were found to inhibit irreversibly the cysteine protease papain. They were selective for cysteine proteases since no inhibition was found for the serine protease chymotrypsin.
Related Articles:
Synthesis of azocine derivatives from thio aldehyde Diels-Alder adducts
[Vedejs, E.; Stults, J. S. Journal of Organic Chemistry, 1988 , vol. 53, # 10 p. 2226 - 2232]
Constrained (l-)-S-adenosyl-l-homocysteine (SAH) analogues as DNA methyltransferase inhibitors
[Isakovic, Ljubomir; Saavedra, Oscar M.; Llewellyn, David B.; Claridge, Stephen; Zhan, Lijie; Bernstein, Naomy; Vaisburg, Arkadii; Elowe, Nadine; Petschner, Andrea J.; Rahil, Jubrail; Beaulieu, Norman; Gauthier, France; MacLeod, A. Robert; Delorme, Daniel; Besterman, Jeffrey M.; Wahhab, Amal Bioorganic and Medicinal Chemistry Letters, 2009 , vol. 19, # 10 p. 2742 - 2746]