173458-82-7

Upstream product

• 64-18-6 formic acid 
• 55817-67-9 (1-benzyl-3-cyano-4,5-diphenyl-1H-pyrrol-2-yl)carbonohydrazonoyl dicyanide 
• 173458-79-2 7-benzyl-5,6-diphenyl-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one 
• 173458-79-2 7-benzyl-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-ol 

Downstream Products

• 1028275-75-3 (7-Benzyl-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)-(3-chloro-phenyl)-amine 
• 173458-88-3 4-chloro-5,6-diphenyl-7H-pyrrolo[2,3-d]pyrimidine 
• 929626-78-8 7-benzyl-5,6-diphenyl-3,7-dihydro-pyrrolo[2,3-d]pyrimidine-4-thione 

Relevant academic research and scientific papers

Synthesis and Kinetic Testing of Tetrahydropyrimidine-2-thione and Pyrrole Derivatives as Inhibitors of the Metallo-β-lactamase from Klebsiella pneumonia and Pseudomonas aeruginosa

Metallo-β-lactamases (MBLs), produced by an increasing number of bacterial pathogens, facilitate the hydrolysis of many commonly used β-lactam antibiotics. There are no clinically useful antagonists against MBLs. Two sets of tetrahydropyrimidine-2-thione and pyrrole derivatives were synthesized and assayed for their inhibitory effects on the catalytic activity of the IMP-1 MBL from Pseudomonas aeruginosa and Klebsiella pneumoniae. Nine compounds tested (1a, 3b, 5c, 6b, 7a, 8a, 11c, 13a, and 16a) showed micromolar inhibition constants (Ki values range from ~20-80μm). Compounds 1c, 2b, and 15a showed only weak inhibition. In silico docking was employed to investigate the binding mode of each enantiomer of the strongest inhibitor, 5c (Ki=19±9μm), as well as 7a (Ki=21±10μm), the strongest inhibitor of the pyrrole series, in the active site of IMP-1.

Identification, SAR studies, and X-ray Co-crystallographic analysis of a novel furanopyrimidine aurora kinase a inhibitor

Herein we reveal a simple method for the identification of novel Aurora kinase A inhibitors through substructure searching of an in-house compound library to select compounds for testing. A hydrazone fragment conferring Aurora kinase activity and heterocy

4-(Phenylamino)pyrrolopyrimidines: Potent and selective, ATP site directed inhibitors of the EGF-receptor protein tyrosine kinase

Using a pharmacophore model for ATP-competitive inhibitors interacting with the active site of the EGF-R protein tyrosine kinase (PTK), 4- (phenylamino)-7H-pyrrolo[2,3-d]pyrimidines have been identified as a novel class of potent EGF-R protein tyrosine kinase inhibitors. In an interactive process, this class of compounds was then optimized. 13, 14, 28, 36, 37, and 44, the most potent compounds of this series, inhibited the EGF-R PTK with IC50 values in the low nanomolar range. High selectivity toward a panel of nonreceptor tyrosine kinases (c-Src, v-Abl) and serine/threonine kinases (PKC α, PKA) was observed. Kinetic analysis revealed competitive type kinetics relative to ATP. In cells, EGF-stimulated cellular tyrosine phosphorylation was inhibited by compounds 13, 36, 37, and 44 at IC50 values between 0.1 and 0.4 μM, whereas PDGF-induced tyrosine phosphorylation was not affected by concentrations up to 10 μM. In addition, these compounds were able to selectively inhibit c-fos mRNA expression in EGF-dependent cell lines with IC50 values between 0.1 and 2 μM, but did not affect c-fos mRNA induction in response to PDGF or PMA (IC50 >100 μM). Proliferation of the EGF- dependent MK cell line was inhibited with similar IC50 values. From SAR studies, a binding mode for 4-(phenylamino)-7H-pyrrolo[2,3-d]pyrimidines as well as for the structurally related 4-(phenylamino)quinazolines at the ATP- binding site of the EGF-R tyrosine kinase is proposed. 4-(Phenylamino)-7H- pyrrolo[2,3-d]pyrimidines therefore represent a new class of highly potent tyrosine kinase inhibitors which preferentially inhibit the EGF-mediated signal transduction pathway and have the potential for further evaluation as anticancer agents.