Preparation Note
Soluble in DMSO. At 1 mg/ml the solution is stable for 1 week at 2-8 °C.
Biochem/physiol Actions
Antibacterial mycotoxin.1 Specific inhibitor of lysine-specific histone methyltransferase making the compound useful in the study of heterochromatin mediated gene repression.2 Selective competitive inhibitor of thioredoxin reductase-1 (TrxR1), a putative mechanism of its anticancer activity.3
methyltransferase making the compound useful in the study of heterochromatin mediated gene repression.2 Selective competitive inhibitor of thioredoxin reductase-1 (TrxR1), a putative mechanism of its anticancer activity.3
General description
Chaetocin is a fungal metabolite with antimicrobial and cytostatic activity.1, 2 It belongs to the 3,6-epidithio-diketopiperazines class of which gliotoxin, sporidesmin, aranotin, oryzachloride, verticillin A and the melinacidins are members.1,3 Chaetocin is a molecular dimer of two five-membered rings cis fused. 1 Interestingly, the chirality of the 3,6-epidithio-diketopiperazine moiety in chaetocin is opposite to the chirality in gliotoxin, sporidesmin, aranotin and oryzachloride and while the later compounds show antiviral activity, chaetocin does not.1 This fungal toxin showed strong cytotoxicity against HeLa cells (IC50=0.05 μg/ml).2 Chaetocin was found to be a specific inhibitor of the lysine-specific histone methyltransferase SU(VAR)3-9 (IC50= 0.6 μM) of Drosophila melanogaster and of its human ortholog (IC50= 0.8 μM), and acts as a competitive inhibitor for S-adenosylmethionine.4 The specificity of chaetocin for SU(VAR)3-9 makes this compound an excellent tool for the study of heterochromatin-mediated gene repression.4References:1. Weber, H. P., et al., The molecular structure and absolute configuration of chaetocin. Acta Cryst., B28, 2945-2951 (1972).2. Udagawa, S., et al., The production of chaetoglobosins, sterigmatocystin, O-methylsterigmatocystin, and chaetocin by Chaetomium spp. and related fungi. Can. J. microbiol., 25, 170-177 (1979).3. Gardiner, D. M., et al., The epipolythiodioxopiperazine (ETP) class of fungal toxins: distribution, mode of action, functions and biosynthesis. Microbiol., 151, 1021-1032 (2005).4. Greiner, D., et al., Identification of a specific inhibitor of the histone methyltransferase SU(VAR)3-9. Nat. Chem. Biol., 1, 143-145 (2005). |
Preparation Note
Soluble in DMSO. At 1 mg/ml the solution is stable for 1 week at 2-8 °C.
Biochem/physiol Actions
Antibacterial mycotoxin.1 Specific inhibitor of lysine-specific histone methyltransferase making the compound useful in the study of heterochromatin mediated gene repression.2 Selective competitive inhibitor of thioredoxin reductase-1 (TrxR1), a putative mechanism of its anticancer activity.3
methyltransferase making the compound useful in the study of heterochromatin mediated gene repression.2 Selective competitive inhibitor of thioredoxin reductase-1 (TrxR1), a putative mechanism of its anticancer activity.3
General description
Chaetocin is a fungal metabolite with antimicrobial and cytostatic activity.1, 2 It belongs to the 3,6-epidithio-diketopiperazines class of which gliotoxin, sporidesmin, aranotin, oryzachloride, verticillin A and the melinacidins are members.1,3 Chaetocin is a molecular dimer of two five-membered rings cis fused. 1 Interestingly, the chirality of the 3,6-epidithio-diketopiperazine moiety in chaetocin is opposite to the chirality in gliotoxin, sporidesmin, aranotin and oryzachloride and while the later compounds show antiviral activity, chaetocin does not.1 This fungal toxin showed strong cytotoxicity against HeLa cells (IC50=0.05 μg/ml).2 Chaetocin was found to be a specific inhibitor of the lysine-specific histone methyltransferase SU(VAR)3-9 (IC50= 0.6 μM) of Drosophila melanogaster and of its human ortholog (IC50= 0.8 μM), and acts as a competitive inhibitor for S-adenosylmethionine.4 The specificity of chaetocin for SU(VAR)3-9 makes this compound an excellent tool for the study of heterochromatin-mediated gene repression.4References:1. Weber, H. P., et al., The molecular structure and absolute configuration of chaetocin. Acta Cryst., B28, 2945-2951 (1972).2. Udagawa, S., et al., The production of chaetoglobosins, sterigmatocystin, O-methylsterigmatocystin, and chaetocin by Chaetomium spp. and related fungi. Can. J. microbiol., 25, 170-177 (1979).3. Gardiner, D. M., et al., The epipolythiodioxopiperazine (ETP) class of fungal toxins: distribution, mode of action, functions and biosynthesis. Microbiol., 151, 1021-1032 (2005).4. Greiner, D., et al., Identification of a specific inhibitor of the histone methyltransferase SU(VAR)3-9. Nat. Chem. Biol., 1, 143-145 (2005). |