18588-50-6

Usage

Uses

Used in Pharmaceutical Industry:
6-Methyl-5-phenyl-2,4-pyrimidinediamine is used as a pharmaceutical agent for its potential therapeutic effects in treating various diseases. Its ability to selectively inhibit specific enzyme targets makes it a promising candidate for the development of novel treatments.
Used in Cancer Treatment:
In the field of oncology, 6-Methyl-5-phenyl-2,4-pyrimidinediamine is used as an anticancer agent. Its inhibitory effects on certain enzymes can potentially contribute to the suppression of tumor growth and the management of cancer progression.
Used in Neurodegenerative Disorders:
6-Methyl-5-phenyl-2,4-pyrimidinediamine is also being investigated for its potential use in the treatment of neurodegenerative disorders. Its enzyme-inhibiting properties may offer new avenues for therapeutic intervention in conditions such as Alzheimer's disease and Parkinson's disease.
Used in Drug Development Research:
In the research and development sector, 6-Methyl-5-phenyl-2,4-pyrimidinediamine serves as a subject of interest for scientists exploring its potential applications and mechanisms of action. Its unique chemical structure and biological activity provide a foundation for designing new drugs and understanding their interactions with biological systems.

InChI:InChI=1/C11H12N4/c1-7-9(8-5-3-2-4-6-8)10(12)15-11(13)14-7/h2-6H,1H3,(H4,12,13,14,15)

Upstream product

• 186581-53-3 diazomethane 
• 4468-48-8 1-phenyl-1-cyanopropan-2-one 
• 22211-32-1 3-Methoxy-2-phenyl-cis-crotononitril 
• 113-00-8 guanidine nitrate 
• 50-01-1 guanidine hydrochloride 
• 506-93-4 guanidine nitrate 

Relevant academic research and scientific papers

COMPOUNDS FOR THE TREATMENT OF LYSOSOMAL STORAGE DISEASES

A method of treating a lysosomal storage disease comprises administering a pyrimethamine derivative to a subject in need thereof.

Structure-based design, synthesis and preliminary evaluation of selective inhibitors of dihydrofolate reductase from Mycobacterium tuberculosis

Tuberculosis is an increasing threat, owing to the spread of AIDS and to the development of resistance of the causative organism, Mycobacterium tuberculosis, to the currently available drugs. Dihydrofolate reductase (DHFR) is an important enzyme of the folate cycle; inhibition of DHFR inhibits growth and causes cell death. The crystal structure of M. tuberculosis DHFR revealed a glycerol tightly bound close to the binding site for the substrate dihydrofolate; this glycerol-binding motif is absent from the human enzyme. A series of pyrimidine-2,4-diamines was designed with a two-carbon tether between a glycerol-mimicking triol and the 6-position of the heterocycle; these compounds also carried aryl substituents at the 5-position. These, their diastereoisomers, analogues lacking two hydroxy groups and analogues lacking the two-carbon spacing linker were synthesised by acylation of the anions derived from phenylacetonitriles with ethyl (4S,5R)-4-benzyloxymethyl-2,2-dimethyl-1,3-dioxolane-4-propanoate, ethyl (4S,5S)-4-benzyloxymethyl-2,2-dimethyl-1,3-dioxolane-4-propanoate, tetrahydrooxepin-2-one and 2,3-O-isopropylidene-d-erythronolactone, respectively, to give the corresponding α-acylphenylacetonitriles. Formation of the methyl enol ethers, condensation with guanidine and deprotection gave the pyrimidine-2,4-diamines. Preliminary assay of the abilities of these compounds to inhibit the growth of TB5 Saccharomyces cerevisiae carrying the DHFR genes from M. tuberculosis, human and yeast indicated that 5-phenyl-6-((3R,4S)-3,4,5-trihydroxypentyl)pyrimidine-2,4-diamine selectively inhibited M. tuberculosis DHFR and had little effect on the human or yeast enzymes.

Development of 2,4-diaminopyrimidines as antimalarials based on inhibition of the S108N and C59R+S108N mutants of dihydrofolate reductase from pyrimethamine resistant Plasmodium falciparum

The reduced binding of pyrimethamine to Serl08Asn (S108N) mutants of parasite dihydrofolate reductase (DHFR), which forms the basis of resistance of Plasmodium falciparum to pyrimethamine, is largely due to steric constraint imposed by the bulky side chain of N108 on Cl of the 5-p-Cl-phenyl group. This and other S108 mutants with bulky side chains all showed reduced binding to pyrimethamine and cycloguanil. Less effect on binding to some bulky mutants was observed for trimethoprim, with greater flexibility for the 5-substituent. S108N DHFR also binds poorly with other pyrimethamine derivatives with bulky groups in place of the p-Cl, and the binding was generally progressively poorer for the double (C59R+S108N) mutant. Removal of the p-Cl or replacement with m-Cl led to better binding with the mutant DHFRs. Pyrimethamine analogues with unbranched hydrophobic 6-substituents showed generally good binding with the mutant DHFRs. A number of compounds were identified with high affinities for both wild-type and mutant DHFRs, with very low to no affinity to human DHFR. Some of these compounds show good antimalarial activities against pyrimethamine-resistant P. falciparum containing the mutant DHFRs with low cytotoxicity to three mammalian cell lines.

SYNTHESES OF 2,4-DIAMINOPYRIMIDINES AND 1-AMINOISOQUINOLINES IN THE REACTIONS OF ALKYL AND BENZYL KETONES WITH CYANAMIDE AND N,N-DIMETHYLCYANAMIDE

The reaction of alkyl and benzyl ketones with cyanamide and N,N-dimethylcyanamide in the presence of POCl3 was examined.At the first stage chloroformamidine derivatives were formed.In the presence of TiCl4, they underwent further reactions to the derivati