203436-09-3

Basic information

• Product Name: 9H-Purin-6-aMine, 2-chloro-N-[(4-Methoxyphenyl)Methyl]-
• Synonyms: 9H-Purin-6-aMine, 2-chloro-N-[(4-Methoxyphenyl)Methyl]-;2-Chloro-N-(4-methoxybenzyl)-9H-purin-6-amine
• CAS NO: 203436-09-3
• Molecular Formula: C₁₃H₁₂ClN₅O
• Molecular Weight: 289.72028
• Mol File: 203436-09-3.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 9H-Purin-6-aMine, 2-chloro-N-[(4-Methoxyphenyl)Methyl]-(CAS DataBase Reference)
• NIST Chemistry Reference: 9H-Purin-6-aMine, 2-chloro-N-[(4-Methoxyphenyl)Methyl]-(203436-09-3)
• EPA Substance Registry System: 9H-Purin-6-aMine, 2-chloro-N-[(4-Methoxyphenyl)Methyl]-(203436-09-3)

Safety Data

• Hazardous Substances Data: 203436-09-3(Hazardous Substances Data)

Upstream product

• 2393-23-9 4-methoxy-benzylamine 
• 5451-40-1 2,6 dichloropurine 

Downstream Products

• 203436-13-9 (2-chloro-9-isopropyl-9H-purin-6-yl)-(4-methoxybenzyl)-amine 
• 203436-18-4 9-benzyl-2-chloro-N-(4-methoxybenzyl)-9H-purin-6-amine 
• 1007556-12-8 2-chloro-6-[(4-methoxybenzyl)amino]-9-cyclopentylpurine 
• 1007556-27-5 9-butyl-2-chloro-N-(4-methoxybenzyl)-9H-purin-6-amine 

Relevant articles and documents

Diaminopurine-acridine heterodimers for specific recognition of abasic site containing DNA. Influence on the biological activity of the position of the linker on the purine ring

Three acridine-diaminopurine heterodimers tethered by a linker containing an N,N′-substituted guanidine were prepared. The molecules differ by the site of introduction of the linker on the 2,6-diaminopurine. The interactions of the new heterodimers with abasic site containing oligonucleotide were compared, and their cytotoxicity was measured in the presence or absence of the antitumor alkylating agent BCNU.

Targeting different binding sites in the CFTR structures allows to synergistically potentiate channel activity

Recent evidence shows that combination of correctors and potentiators, such as the drug ivacaftor (VX-770), can significantly restore the functional expression of mutated Cystic Fibrosis Transmembrane conductance Regulator (CFTR), an anion channel which is mutated in cystic fibrosis (CF). The success of these combinatorial therapies highlights the necessity of identifying a broad panel of specific binding mode modulators, occupying several distinct binding sites at structural level. Here, we identified two small molecules, SBC040 and SBC219, which are two efficient cAMP-independent potentiators, acting at low concentration of forskolin with EC50 close to 1 μM and in a synergic way with the drug VX-770 on several CFTR mutants of classes II and III. Molecular dynamics simulations suggested potential SBC binding sites at the vicinity of ATP-binding sites, distinct from those currently proposed for VX-770, outlining SBC molecules as members of a new family of potentiators.

COMPOUNDS FOR TREATING CYSTIC FIBROSIS

The present invention relates to compounds of Formula (I) or pharmaceutically acceptable enantiomers, salts, solvates or prodrugs thereof. The invention further relates to the use of the compounds of Formula (I) for the treatment of cystic fibrosis. The invention also relates to a process for manufacturing compounds of Formula (I).

Development of potent purine-derived nitrile inhibitors of the trypanosomal protease TbcatB

Human African trypanosomiasis (HAT), a major health concern in sub-Saharan Africa, is caused by the protozoan parasite Trypanosoma brucei. Recent studies have shown that a cathepsin B like protease, TbcatB, is essential to the survival of T. brucei in vit

Purine inhibitors of cyclin dependent kinase 2

A 2,6,9-trisubstituted purine composition having the following formula: STR1 where X is a amino, oxo, thio, of sulfone moiety, R1 is a lower alkyl, substituted lower alkyl, cycloalkyl, substituted cycloalkyl, cycloheteroalkyl, substituted cyclo

Synthesis and activity of 2,6,9-trisubstituted purines

The preparation of a series of 2,6,9-trisubstituted purines and the structure-activity data for the inhibition of cyclin dependent kinase, CDK2 are presented.