Compounds > Diosmetin-7-O-beta-D-glucopyranoside

Diosmetin-7-O-beta-D-glucopyranoside and mangostin

Diosmetin-7-O-beta-D-glucopyranoside has been researched along with mangostin* in 1 studies

Other Studies

1 other study(ies) available for Diosmetin-7-O-beta-D-glucopyranoside and mangostin

Article	Year
Discovery of α-mangostin as a novel competitive inhibitor against mutant isocitrate dehydrogenase-1. Bioorganic & medicinal chemistry letters, 2015, Dec-01, Volume: 25, Issue:23 Somatic heterozygous mutations of isocitrate dehydrogenase-1 (IDH1) are abundantly found in several types of cancer and strongly implicate altered metabolism in carcinogenesis. In the present study, we have identified α-mangostin as a novel selective inhibitor of mutant IDH1 (IDH1-R132H). We have observed that α-mangostin competitively inhibits the binding of α-ketoglutarate (α-KG) to IDH1-R132H. The structure-relationship study reveals that α-mangostin exhibits the strongest core inhibitor structure. Finally, we have observed that α-mangostin selectively promotes demethylation of 5-methylcytosine (5mC) and histone H3 trimethylated lysine residues in IDH1 (+/R132H) MCF10A cells, presumably via restoring the activity of cellular α-KG-dependent DNA hydroxylases and histone H3 lysine demethylases. Collectively, we provide evidence that α-mangostin selectively inhibits IDH1-R132H. Topics: Binding, Competitive; Drug Discovery; Humans; Isocitrate Dehydrogenase; MCF-7 Cells; Molecular Structure; Mutation; Recombinant Proteins; Structure-Activity Relationship; Xanthones	2015

Article

Year

Discovery of α-mangostin as a novel competitive inhibitor against mutant isocitrate dehydrogenase-1.

Bioorganic & medicinal chemistry letters, 2015, Dec-01, Volume: 25, Issue:23

Somatic heterozygous mutations of isocitrate dehydrogenase-1 (IDH1) are abundantly found in several types of cancer and strongly implicate altered metabolism in carcinogenesis. In the present study, we have identified α-mangostin as a novel selective inhibitor of mutant IDH1 (IDH1-R132H). We have observed that α-mangostin competitively inhibits the binding of α-ketoglutarate (α-KG) to IDH1-R132H. The structure-relationship study reveals that α-mangostin exhibits the strongest core inhibitor structure. Finally, we have observed that α-mangostin selectively promotes demethylation of 5-methylcytosine (5mC) and histone H3 trimethylated lysine residues in IDH1 (+/R132H) MCF10A cells, presumably via restoring the activity of cellular α-KG-dependent DNA hydroxylases and histone H3 lysine demethylases. Collectively, we provide evidence that α-mangostin selectively inhibits IDH1-R132H.

Topics: Binding, Competitive; Drug Discovery; Humans; Isocitrate Dehydrogenase; MCF-7 Cells; Molecular Structure; Mutation; Recombinant Proteins; Structure-Activity Relationship; Xanthones

2015