18346-05-9Relevant academic research and scientific papers
Cs2CO3-Promoted Direct N-Alkylation: Highly Chemoselective Synthesis of N-Alkylated Benzylamines and Anilines
Castillo, Juan-Carlos,Orrego-Hernández, Jessica,Portilla, Jaime
, p. 3824 - 3835 (2016/08/20)
Herein is described an efficient and chemoselective method for the synthesis of diversely substituted secondary amines in yields up to 98 %. Direct mono-N-alkylation of primary benzylamines and anilines with a wide range of alkyl halides is promoted by a cesium base in the absence of any additive or catalyst. The basicity and solubility of cesium carbonate in anhydrous N,N-dimethylformamide not only enables mono-N-alkylation of primary amines but also suppresses undesired dialkylation of the desired amines.
Direct N9-arylation of purines with aryl halides
Larsen, Anders Foller,Ulven, Trond
supporting information, p. 4997 - 4999 (2014/05/06)
An efficient method for N-arylation of purines is reported. The N-arylation is catalysed by Cu(i) and 4,7-bis(2-hydroxyethylamino)-1,10-phenanthroline (BHPhen) in aqueous DMF or ethanol. The reaction generally proceeds with high selectivity for the N
Synthesis and biological testing of purine derivatives as potential ATP-competitive kinase inhibitors
Laufer, Stefan A.,Domeyer, David M.,Scior, Thomas R. F.,Albrecht, Wolfgang,Hauser, Dominik R. J.
, p. 710 - 722 (2007/10/03)
On the basis of ATP adenine, a series of adenine and purine derivatives was prepared and tested for their ability to inhibit a spectrum of disease-related kinases. There has been scant research investigating the potential of cosubstrate derived kinase inhibitors for other kinases than CDKs. Our inhibitor design combined the purine system from the original cosubstrate ATP and phenyl moieties in order to explore possible interactions with the different regions of the ATP binding site in several disease-related protein kinases. There have been a number of hits for the assayed substances, which led us to conclude that the spectrum of compounds may prove to be a valuable tool kit for the evaluation of bonding and selectivity patterns for a wide variety of kinases.
