115974-97-5Relevant articles and documents
Reduction of Electron-Deficient Alkenes Enabled by a Photoinduced Hydrogen Atom Transfer
Larionova, Natalia A.,Ondozabal, Jun Miyatake,Cambeiro, Xacobe C.
, p. 558 - 564 (2021)
Direct hydrogen atom transfer from a photoredox-generated Hantzsch ester radical cation to electron-deficient alkenes has enabled the development of an efficient formal hydrogenation under mild, operationally simple conditions. The HAT-driven mechanism is supported by experimental and computational studies. The reaction is applied to a variety of cinnamate derivatives and related structures, irrespective of the presence of electron-donating or electron-withdrawing substituents in the aromatic ring and with good functional group compatibility. (Figure presented.).
HISTONE DEACETYLASE 6 INHIBITORS AND METHOD FOR TREATING NEUROPATHIC PAIN
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, (2021/01/29)
Disclosed herein are hydroxamic acid compounds. Also disclosed is a method of using the hydroxamic acid compounds for treating a condition associated with histone deacetylase 6.
Design, synthesis and biological evaluation of quinoline derivatives as HDAC class I inhibitors
Chen, Chen,Hou, Xuben,Wang, Guohua,Pan, Wenyan,Yang, Xinying,Zhang, Yingkai,Fang, Hao
, p. 11 - 23 (2017/04/06)
Inhibition of histone deacetylase (HDAC) has been regarded as a potential therapeutic approach for treatment of multiple diseases including cancer. Based on pharmacophore model of HDAC inhibitors, a series of quinoline-based N-hydroxycinnamamides and N-hydroxybenzamides were designed and synthesized as potent HDAC inhibitors. All target compounds were evaluated for their in?vitro HDAC inhibitory activities and anti-proliferative activities and the best compound 4a surpass Vorinostat in both enzymatic inhibitory activity and cellular anti-proliferative activity. In terms of HDAC isoforms selectivity, compounds 4a exhibited preferable inhibition for class I HDACs, especially for HDAC8, the IC50 value (442?nM) was much lower than that of Vorinostat (7468?nM). Subsequently, we performed class I & IIa HDACs whole cell enzyme assay to evaluate inhibitory activity in whole cell context. Compounds 4a and 4e displayed much better cellular activity for class I HDACs than that for class IIa HDACs, which indicated that 4a and 4e might be potent class I HDAC inhibitors. Meanwhile, flow cytometry analysis showed that compound 4a and 4e can promote cell apoptosis in?vitro.