3602-98-0

Upstream product

• 10255-95-5 2-phenylmalonamide 
• 141-78-6 ethyl acetate 
• 124-42-5 acetamidine hydrochloride 
• 83-13-6 diethyl 2-phenylmalonate 

Downstream Products

• 31778-27-5 4,6-dichloro-2-methyl-5-phenylpyrimidine 
• 1240108-36-4 4,6-dibromo-2-methyl-5-phenyl-pyrimidine 
• 945716-95-0 4-chloro-5-(4-chlorophenyl)-6-phenylethynylpyrimidine 
• 945716-86-9 [4-(6-chloro-2-methyl-5-phenylpyrimidin-4-ylethynyl)phenyl]dimethylamine 

Relevant academic research and scientific papers

FUSED PYRIMIDINES AS AKT INHIBITORS

The present invention relates to compounds of formula (I), a N-oxide or tautomer or stereoisomer thereof, or a salt thereof, wherein ring B and the imidazole to which it is fused, R4, R6, R7, R10, m and n have the meanings as given in the description and the claims, which are effective inhibitors of the Pi3K/Akt pathway, processes for their production and their use as pharmaceuticals.

4-Amino-5-aryl-6-arylethynylpyrimidines: Structure-activity relationships of non-nucleoside adenosine kinase inhibitors

A series of non-nucleoside adenosine kinase (AK) inhibitors is reported. These inhibitors originated from the modification of 5-(3-bromophenyl)-7-(6-morpholin-4-ylpyridin-3-yl)pyrido[2,3-d]pyrimidin-4-ylamine (ABT-702). The identification of a linker that would approximate the spatial arrangement found between the pyrimidine ring and the aryl group at C(7) in ABT-702 was a key element in this modification. A search of potential linkers led to the discovery of an acetylene moiety as a suitable scaffold. It was hypothesized that the aryl acetylenes, ABT-702, and adenosine bound to the active site of AK (closed form) in a similar manner with respect to the orientation of the heterocyclic base. Although potent acetylene analogs were discovered based on this assumption, an X-ray crystal structure of 5-(4-dimethylaminophenyl)-6-(6-morpholin-4-ylpyridin-3-ylethynyl)pyrimidin-4-ylamine (16a) revealed a binding orientation contrary to adenosine. In addition, this compound bound tightly to a unique open conformation of AK. The structure-activity relationships and unique ligand orientation and protein conformation are discussed.