27845-53-0Relevant articles and documents
Ni-catalyzed reductive decyanation of nitriles with ethanol as the reductant
Wu, Ke,Ling, Yichen,Sun, Nan,Hu, Baoxiang,Shen, Zhenlu,Jin, Liqun,Hu, Xinquan
supporting information, p. 2273 - 2276 (2021/03/09)
A nickel-catalyzed reductive decyanation of aromatic nitriles has been developed, in which the readily available and abundant ethanol was applied as the hydride donor. Various functional groups on the aromatic rings, such as alkoxyl, amino, imino and amide, were compatible in this catalytic protocol. Heteroaryl, benzylic and alkenyl nitriles were also tolerated. Mechanistic investigation indicated that ethanol provided hydride efficientlyviaβ-hydride elimination in this reductive decyanation.
Synthesis and molecular docking studies of imines as α-glucosidase and α-amylase inhibitors
Aispuro-Pérez, Analy,Bastidas, Pedro,Calderón-Zamora, Loranda,García-Páez, Fernando,López-ávalos, Juan,Monta?o, Sarita,Montes-Avila, Julio,Ochoa-Terán, Adrián,Osuna-Martínez, Ulises,Picos-Corrales, Lorenzo A.,Sarmiento-Sánchez, Juan I.
, (2019/12/25)
Imine functionality is found in many compounds with important biological activity. Thus, the development of novel synthetic approaches for imines is important. In this work, it is propose an easy, eco-friendly and straightforward synthesis pathway of aryl imines under microwave irradiation catalyzed by Alumina-sulfuric acid. In addition, the in vitro enzymatic inhibition, antioxidant activity and molecular docking studies were performed. The aryl imines were isolated with yields in the range of 37–94%. All aryl imines synthesized were evaluated for in vitro inhibitory potential against α-glucosidase and α-amylase enzymes and the results exhibited that the most of the compounds displayed inhibitory activity against both enzymes. The (E)-1-(4-nitrophenyl)-N-(pyridin-2-yl)methanimine (3d) was 1.15-fold more active than acarbose against α-amylase whilst the (E)-1-phenyl-N-(pyridin-2-yl)methanimine (3c) displayed similar activity that acarbose against α-glucosidase. The molecular docking studies in α-glucosidase and α-amylase reveal that aryl imines mainly establish an H-bond with the R2-subtituent and hydrophobic interactions with the R1-subtituent. The docking analysis reveals these synthetic aryl imines 3d-i interact in same active site than acarbose drug in both enzymes.
A BEt3-Base catalyst for amide reduction with silane
Yao, Wubing,Fang, Huaquan,He, Qiaoxing,Peng, Dongjie,Liu, Guixia,Huang, Zheng
, (2019/05/22)
Reported herein is the development of a simple but practical catalytic system for the selective reduction of amides with hydrosilane or hydrosiloxane. Low-cost and readily available triethylborane (1.0 M in THF), in combination with a catalytic amount of an alkali metal base, was found to catalyze the reduction of all three amide classes (tertiary, secondary, and primary amides) to form amines under mild conditions. In addition, the selective transformation of secondary amides to aldimines and primary amides to nitriles can also be achieved by using a proper combination of BEt3 and base. The scope of these BEt3-base-catalyzed amide hydrosilylation reactions has been explored in depth. Preliminary results of mechanistic studies suggest a modified Piers' silane Si-H···B activation mode wherein the hydride abstraction by BEt3 is promoted by the coordination of an alkoxide or hydroxide anion to the Si center.
