39208-61-2Relevant academic research and scientific papers
Electrochemical NaI/NaCl-mediated one-pot synthesis of 2-aminobenzoxazoles in aqueous mediaviatandem addition-cyclization
Huynh, Thao Nguyen Thanh,Koguchi, Shinichi,Rerkrachaneekorn, Tanawat,Sukwattanasinitt, Mongkol,Tankam, Theeranon,Wacharasindhu, Sumrit
supporting information, p. 5189 - 5194 (2021/07/29)
An electrochemical synthesis of 2-aminobenzoxazoles from 2-aminophenols and isothiocyanates was successfully developed in a one-pot fashion. Using inexpensive and widely available NaI and NaCl co-operatively in catalytic amounts, our electrosynthesis approach provided various 2-aminobenzoxazole products in moderate to high yields in an open-flask type undivided cell without using any external supporting electrolyte and base. The protocol can be applied to the synthesis of 2-aminobenzothiazoles from the corresponding 2-thiophenols in moderate yields. This protocol has many benefits. It is metal-free and highly scalable and uses inexpensive mediators and EtOH/water as an environmentally friendly solvent under mild conditions.
Environment-friendly and efficient synthesis of 2-aminobenzo-xazoles and 2-aminobenzothiazoles catalyzed by: Vitreoscilla hemoglobin incorporating a cobalt porphyrin cofactor
Li, Fengxi,Li, Zhengqiang,Su, Jiali,Wang, Chunyu,Wang, Ciduo,Wang, Lei,Xu, Yaning,Zhao, Nan
, p. 8047 - 8052 (2021/11/01)
In this study, an environment-friendly and efficient artificial Vitreoscilla hemoglobin (VHb) for the synthesis of 2-aminobenzoxazoles and 2-aminobenzothiazoles has been reported. We demonstrate an expression-based porphyrin substitution strategy to produce VHb containing cobalt porphyrin instead of native hemin, which can catalyze the oxidative cyclization of corresponding 2-aminobenzoxazoles and 2-aminobenthiazoles with up to 97% yield and 4850 catalytic turnovers in water under aerobic conditions. Hence, we provide a green and mild method for the synthesis of 2-aminobenzoxazoles and 2-aminobenzothiazoles. In addition, we indicate the value of porphyrin ligand substitution as a strategy to tune and enhance the catalytic properties of hemoproteins in non-natural reactions.
A Cu2O/TBAB-promoted approach to synthesize heteroaromatic 2-Amines: Via one-pot cyclization of aryl isothiocyanates with ortho-substituted amines in water
Chen, Ling,Dong, Yibo,Wu, Yangjie,Yang, Jinchen,Zhang, Jinli
supporting information, p. 7425 - 7430 (2020/10/13)
An efficient approach to synthesize heteroaromatic 2-Amines from one-pot desulfurization/dehydrogenative cyclization of aryl isothiocyanates with ortho-substituted amines in water was developed. This approach tolerated a wide range of functional groups on
Synthesis of N-aryl-2-aminobenzoxazoles from substituted benzoxazole-2-thiol and 2-chloro-N-arylacetamides in KOH-DMF system
Wang, Guang-Cheng,Wang, Jing,Li, Lu-Yao,Chen, Shan,Peng, Ya-Ping,Xie, Zhen-Zhen,Chen, Ming,Deng, Bin,Li, Wen-Biao
, p. 1257 - 1268 (2017/07/18)
A simple and novel method for the synthesis of N-aryl-2-aminobenzoxazoles from substituted benzoxazole-2-thiol and 2-chloro-N-arylacetamides in KOH-DMF system has been developed. The present protocol provides an attractive approach to access various N-aryl-2-aminobenzoxazoles in moderate to good yields without using transition metal catalyst under very mild reaction condition.
Synthesis, biological evaluation and molecular docking study of N-arylbenzo[d]oxazol-2-amines as potential α-glucosidase inhibitors
Wang, Guangcheng,Peng, Zhiyun,Wang, Jing,Li, Juan,Li, Xin
, p. 5374 - 5379 (2016/10/22)
A novel series of N-arylbenzo[d]oxazol-2-amines (4a–4m) were synthesized and evaluated for their α-glucosidase inhibitory activity. Compounds 4f–4i, 4k and 4m displayed potent inhibitory activity against α-glucosidase with IC50values in the range of 32.49?±?0.17–120.24?±?0.51?μM as compared to the standard drug acarbose. Among all tested compounds, compound 4g having 4-phenoxy substitution at the phenyl ring was found to be the most active inhibitor of α-glucosidase with an IC50value of 32.49?±?0.17?μM. Analysis of the kinetics of enzyme inhibition indicated that compound 4g is a noncompetitive inhibitor of α-glucosidase with a Kivalue of 31.33?μM. Binding interaction of compound 4g with α-glucosidase was explored by molecular docking simulation.
