25373-69-7Relevant articles and documents
A strong hydride donating, acid stable and reusable 1,4-dihydropyridine for selective aldimine and aldehyde reductions
Hirao, Yasukazu,Eto, Hajime,Teraoka, Mitsuru,Kubo, Takashi
supporting information, p. 1671 - 1679 (2022/03/02)
A 1,4-dihydropyridine derivative, lacking carbonyl groups and containing bulky aryl substituents, was synthesized and found to have a high hydride donating ability, acid resistance and reusability. Thermodynamic parameters for electron and hydride transfer in the redox system comprising the 1,4-dihydropyridine and its corresponding pyridinium ion were determined. In addition, studies showed that the 1,4-dihydropyridine with steric hindrance can be used to promote efficient, boron trifluoride catalyzed selective reduction reactions of aldimines and aldehydes under mild conditions.
Interaction of the dihydropyridine/pyridinium redox pair fixed into a V-shaped conformation
Hirao, Yasukazu,Teraoka, Mitsuru,Kubo, Takashi
, p. 1345 - 1353 (2019/12/23)
A new V-shaped molecule incorporating a dihydropyridine and a pyridinium moiety was synthesized and evaluated for its effect on the interaction between the hydride donor-acceptor pair. Spectroscopic, electrochemical, and computational studies have revealed the presence of the charge transfer interaction as a consequence of the electron donor-acceptor association.
Inhibition of cancer-associated mutant isocitrate dehydrogenases: Synthesis, structure-activity relationship, and selective antitumor activity
Liu, Zhen,Yao, Yuan,Kogiso, Mari,Zheng, Baisong,Deng, Lisheng,Qiu, Jihui J.,Dong, Shuo,Lv, Hua,Gallo, James M.,Li, Xiao-Nan,Song, Yongcheng
supporting information, p. 8307 - 8318 (2014/12/11)
Mutations of isocitrate dehydrogenase 1 (IDH1) are frequently found in certain cancers such as glioma. Different from the wild-type (WT) IDH1, the mutant enzymes catalyze the reduction of α-ketoglutaric acid to d-2-hydroxyglutaric acid (D2HG), leading to cancer initiation. Several 1-hydroxypyridin-2-one compounds were identified to be inhibitors of IDH1(R132H). A total of 61 derivatives were synthesized, and their structure-activity relationships were investigated. Potent IDH1(R132H) inhibitors were identified with Ki values as low as 140 nM, while they possess weak or no activity against WT IDH1. Activities of selected compounds against IDH1(R132C) were found to be correlated with their inhibitory activities against IDH1(R132H), as well as cellular production of D2HG, with R2 of 0.83 and 0.73, respectively. Several inhibitors were found to be permeable through the blood-brain barrier in a cell-based model assay and exhibit potent and selective activity (EC50 = 0.26-1.8 μM) against glioma cells with the IDH1 R132H mutation.