312513-29-4Relevant articles and documents
Synthesis of isoflavones by tandem demethylation and ring-opening/cyclization of methoxybenzoylbenzofurans
Kunyane, Phaladi,Sonopo, Molahlehi S.,Selepe, Mamoalosi A.
, p. 3074 - 3082 (2019/11/19)
The unexpected conversion of benzoylbenzofurans into isoflavones through an intramolecular cascade that involves deprotection and ring-opening/cyclization is described. This was discovered in an investigation of the possible transformation of benzoylbenzofurans into coumaronochromones. This route affords isoflavones in two major steps from acetophenones and benzoquinones. The transformation was validated by synthesizing differently substituted isoflavone derivatives and further applied to a concise synthesis of a potential anticancer lead compound, glaziovianin A (1).
Identification of benzofuran-3-yl(phenyl)methanones as novel SIRT1 inhibitors: Binding mode, inhibitory mechanism and biological action
Wu, Jiahui,Li, Yi,Chen, Kaixian,Jiang, Hualiang,Xu, Ming-Hua,Liu, Dongxiang
, p. 441 - 450 (2013/03/29)
SIRT1 is a NAD+-dependent deacetylase. Here we described new SIRT1 inhibitors with the scaffold of benzofuran-3-yl(phenyl)methanone. The inhibitors were predicted to bind in C-pocket of SIRT1, forming hydrophobic interactions with Phe273, Phe312 and Ile347. Introducing hydroxyl to meta position of phenyl may form H-bond with Asn346. Indeed, (2,5-dihydroxyphenyl)(5- hydroxy-1-benzofuran-3-yl)methanone (16), an analogue with hydroxyls at ortho and meta positions, showed greater inhibition. The binding mode was validated by structural modifications and kinetic studies. Since C-pocket is the site where the nicotinamide moiety of NAD+ binds and the hydrolysis takes place, binding of 16 in C-pocket would block the transformation of NAD+ to productive conformation and hence inhibit the deacetylase activity. Consistently, 16 inhibited SIRT1 through up-regulating p53 acetylation on cellular level.
