6455-00-1Relevant academic research and scientific papers
Synthesis and applications of benzisoselenazolone modified nitrosourea compound
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Paragraph 0082; 0083; 0084; 0085; 0086; 0087; 0088;0129-0133, (2017/08/29)
The present invention relates to a benzisoselenazolone modified nitrosourea compound and applications thereof, wherein the benzisoselenazolone modified nitrosourea compound is represented by a general formula I, has excellent antitumor activity, and can be widely used for preparing antitumor drugs. The general formula I is defined in the specification.
Inhibition of thioredoxin reductase by a novel series of bis-1,2-benzisoselenazol-3(2H)-ones: Organoselenium compounds for cancer therapy
He, Jie,Li, Dongdong,Xiong, Kun,Ge, Yongjie,Jin, Hongwei,Zhang, Guozhou,Hong, Mengshi,Tian, Yongliang,Yin, Jin,Zeng, Huihui
experimental part, p. 3816 - 3827 (2012/08/27)
Thioredoxin reductase (TrxR) is critical for cellular redox regulation and is involved in tumor proliferation, apoptosis and metastasis. Its C-terminal redox-active center contains a cysteine (Cys497) and a unique selenocysteine (Sec498), which are exposed to solvent and easily accessible. Thus, it is becoming an important target for anticancer drugs. Selective inhibition of TrxR by 1,2-(bis-1,2-benzisoselenazol-3(2H)-one)ethane (4a) prevents proliferation of several cancer cell lines both in vivo and in vitro. Using the structure of 4a as a starting point, a series of novel bis-1,2-benzisoselenazol-3(2H)-ones was designed, prepared and tested to explore the structure-activity relationships (SARs) for this class of inhibitor and to improve their potency. Notably, 1,2-(5,5′-dimethoxybis(1,2-benzisoselenazol-3(2H)-one))ethane (12) was found to be more potent than 4a in both in vitro and in vivo evaluation. Its binding sites were confirmed by biotin-conjugated iodoacetamide assay and a SAR model was generated to guide further structural modification.
Substituent effects upon the catalytic activity of aromatic cyclic seleninate esters and spirodioxyselenuranes that act as glutathione peroxidase mimetics
Press, David J.,Mercier, Eric A.,Kuzma, Dusan,Back, Thomas G.
, p. 4252 - 4255 (2008/09/20)
(Chemical Equation Presented) Substituent effects were studied in a series of aromatic cyclic seleninate esters and spirodioxyselenuranes that function as mimetics of the antioxidant selenoenzyme glutathione peroxidase. The methoxy-substituted selenurane proved the most efficacious catalyst for the reduction of hydrogen peroxide with benzyl thiol, and the reaction rates were enhanced for both classes by electron-donating substituents. Hammett plots indicated ρ = -0.45 and -3.1 for the seleninates and selenuranes, respectively, suggesting that oxidation at Se is the rate-determining step in their catalytic cycles.
