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]

More Articles...