Isothiazolones; thiol-reactive inhibitors of cysteine protease cathepsin B and histone acetyltransferase PCAFWisastra, R., Ghizzoni, M., Maarsingh, H., Minnaard, A. J., Haisma, H. J. & Dekker, F. J., 2011, In : Organic and Biomolecular Chemistry. 9, 6, p. 1817-1822 6 p.
Research output: Contribution to journal › Article › Academic › peer-review
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.
|Number of pages||6|
|Journal||Organic and Biomolecular Chemistry|
|Publication status||Published - 2011|
- BIOTINYLATED AFFINITY LABEL, NF-KAPPA-B, INFLAMMATION