6303-46-4

Usage

Uses

Used in Pharmaceutical Industry:
6-chloro-N-(3,4-dichlorophenyl)pyrimidin-4-amine is utilized as a pharmaceutical intermediate for the synthesis of various therapeutic agents. Its unique structure allows it to be a key component in the development of drugs targeting specific biological pathways or receptors, potentially leading to new treatments for a range of diseases.
Used in Agrochemical Industry:
In the agrochemical sector, 6-chloro-N-(3,4-dichlorophenyl)pyrimidin-4-amine serves as a precursor in the production of pesticides or herbicides. Its chemical properties may contribute to the creation of compounds that effectively control pests or unwanted plant growth, thereby enhancing crop yields and agricultural productivity.
Used in Materials Science:
6-chloro-N-(3,4-dichlorophenyl)pyrimidin-4-amine is employed in materials science for the development of novel materials with specific properties. Its incorporation into polymers or other materials could lead to advancements in areas such as electronics, coatings, or specialty chemicals, where unique characteristics are required.
Given the compound's diverse potential applications, further research and testing are essential to fully explore its benefits and to assess any associated risks. This will ensure that 6-chloro-N-(3,4-dichlorophenyl)pyrimidin-4-amine can be safely and effectively integrated into various industries.

Upstream product

• 1193-21-1 4,6-dichloropyrimidine 
• 95-76-1 m,p-dichloroaniline 

Downstream Products

• 1228298-37-0 3-[6-(3,4-dichlorophenylamino)pyrimidin-4-yl]-benzoic acid methyl ester 
• 1228298-38-1 2-[6-(3,4-dichlorophenylamino)pyrimidin-4-yl]-benzamide 

Relevant academic research and scientific papers

Development of a series of aryl pyrimidine kynurenine monooxygenase inhibitors as potential therapeutic agents for the treatment of Huntingtons disease

We report on the development of a series of pyrimidine carboxylic acids that are potent and selective inhibitors of kynurenine monooxygenase and competitive for kynurenine. We describe the SAR for this novel series and report on their inhibition of KMO activity in biochemical and cellular assays and their selectivity against other kynurenine pathway enzymes. We describe the optimization process that led to the identification of a program lead compound with a suitable ADME/PK profile for therapeutic development. We demonstrate that systemic inhibition of KMO in vivo with this lead compound provides pharmacodynamic evidence for modulation of kynurenine pathway metabolites both in the periphery and in the central nervous system.

Discovery of novel Bcr-Abl inhibitors targeting myristoyl pocket and ATP site

Bcr-Abl plays an essential role in the pathogenesis and development of chronic myeloid leukaemia (CML). Inhibition of Bcr-Abl has great potential for therapeutic intervention in CML. In order to obtain novel and potent Bcr-Abl inhibitors, twenty seven 4,6-disubstituted pyrimidines were synthesized and evaluated herein. The biological results indicated that four compounds of them (C4, C5, C16, and C23) were potent Bcr-Abl inhibitors which were comparable to positive control. Moreover, C4 and C5 displayed promising antiproliferative activity against K562 cells. The results suggested that these 4,6-disubstituted pyrimidines could serve as promising leads for further optimization of Bcr-Abl inhibitors.

Binding or bending: Distinction of allosteric abl kinase agonists from antagonists by an NMR-based conformational assay

Allosteric inhibitors of Bcr-Abl have emerged as a novel therapeutic option for the treatment of CML. Using fragment-based screening, a search for novel Abl inhibitors that bind to the myristate pocket was carried out. Here we show that not all myristate ligands are functional inhibitors, but that the conformational state of C-terminal helix-I is a structural determinant for functional activity. We present an NMR-based conformational assay to monitor the conformation of this crucial helix-I and show that myristate ligands that bend helix-I are functional antagonists, whereas ligands that bind to the myristate pocket but do not induce this conformational change are kinase agonists. Activation of c-Abl by allosteric agonists has been confirmed in a biochemical assay.