1775-98-0Relevant articles and documents
Convenient synthesis of flavanone derivatives via oxa-Michael addition using catalytic amount of aqueous cesium fluoride
Miura, Motofumi,Shigematsu, Karin,Toriyama, Masaharu,Motohashi, Shigeyasu
supporting information, (2021/10/25)
A total of 36 flavanones, which included polycyclic aromatic and heterocyclic rings, were readily synthesized via oxa-Michael addition from the corresponding hydroxychalcones with a catalytic amount of aqueous cesium fluoride solution under mild conditions. This method could be applied to the scalable synthesis of eriodictyol as a known potent inhibitor of the SARS-CoV-2 spike protein.
From Carbamate to Chalcone: Consecutive Anionic Fries Rearrangement, Anionic Si → C Alkyl Rearrangement, and Claisen-Schmidt Condensation
Kumar, Singam Naveen,Bavikar, Suhas Ravindra,Pavan Kumar, Chebolu Naga Sesha Sai,Yu, Isaac Furay,Chein, Rong-Jie
supporting information, p. 5362 - 5366 (2018/09/12)
A highly efficient one-pot procedure was developed for the synthesis of various 2′-hydroxychalcones from phenyl diethylcarbamate, featuring consecutive Snieckus-Fries rearrangement, anionic Si a?' C alkyl rearrangement, and Claisen-Schmidt condensation in a single operation. The applicability of this protocol was demonstrated by the highly efficient synthesis of the anti-inflammatory natural product lonchocarpin. The mechanism insight is also provided.
Rapid synthesis of flavone-based monoamine oxidase (MAO) inhibitors targeting two active sites using click chemistry
Jia, Wei Zhen,Cheng, Feng,Zhang, Yin Jun,Ge, Jin Yan,Yao, Shao Q.,Zhu, Qing
, p. 141 - 151 (2016/12/16)
A new library of flavone derivatives targeting two active sites of monoamine oxidases (“aromatic cage” and substrate cavity) were designed and synthesized using click chemistry (CuAAC reaction) between 6-N3-2-phenyl chromones (Az1–Az2) and a series of alkynes (k1–k20). Their inhibitory activities against MAO isoforms (MAO-A and MAO-B) are evaluated. Compounds with fluorine, amide bonds, or amino bonds have shown better inhibition. The most potent flavone MAO inhibitor studied is Az2k19 (1.6?μm for MAO-A, 2.1?μm for MAO-B), while Az1k15 and Az2k15 displayed better selectivity toward MAO-B (SI?>?10). Docking studies are in accordance with our hypothesis that these inhibitors are most likely located at both the substrate cavity and the “aromatic cage”. Our results show that it is considerable to develop new MAO inhibitors from C6 substitution of flavone derivatives and that these compounds are also potential for the treatment of diseases associated with MAOs.