Abstract
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.
Original language | English |
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Pages (from-to) | 1817-1822 |
Number of pages | 6 |
Journal | Organic and Biomolecular Chemistry |
Volume | 9 |
Issue number | 6 |
DOIs | |
Publication status | Published - 2011 |
Keywords
- BIOTINYLATED AFFINITY LABEL
- NF-KAPPA-B
- INFLAMMATION
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CCDC 763229: Experimental Crystal Structure Determination
Wisastra, R. (Contributor), Ghizzoni, M. (Contributor), Maarsingh, H. (Contributor), Minnaard, A. (Contributor), Haisma, H. J. (Contributor) & Dekker, F. J. (Contributor), University of Groningen, 25-Jan-2010
DOI: 10.5517/cctm69x
Dataset
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CCDC 763228: Experimental Crystal Structure Determination
Wisastra, R. (Contributor), Ghizzoni, M. (Contributor), Maarsingh, H. (Contributor), Minnaard, A. (Contributor), Haisma, H. J. (Contributor) & Dekker, F. J. (Contributor), University of Groningen, 25-Jan-2010
DOI: 10.5517/cctm68w
Dataset