Isothiazolones; thiol-reactive inhibitors of cysteine protease cathepsin B and histone acetyltransferase PCAF

Rosalina Wisastra, Massimo Ghizzoni, Harm Maarsingh, Adriaan J. Minnaard, Hidde J. Haisma, Frank J. Dekker*

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

19 Citaten (Scopus)
41 Downloads (Pure)


Isothiazolones and 5-chloroisothiazolones react chemoselectively with thiols by cleavage of the weak nitrogen-sulfur bond to form disulfides. They show selectivity for inhibition of the thiol-dependent cysteine protease cathepsin B and the histone acetyltransferase p300/CBP associated factor (PCAF) based on their substitution pattern. Furthermore, enzyme kinetics and mass spectroscopy indicate covalent binding of a 5-chloroisothiazolone to cathepsin B, which demonstrates their potential utility as probes for activity-based protein profiling.

Originele taal-2English
Pagina's (van-tot)1817-1822
Aantal pagina's6
TijdschriftOrganic and Biomolecular Chemistry
Nummer van het tijdschrift6
StatusPublished - 2011

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