105538-79-2

Upstream product

• 68240-43-7 4,6-dichloro-3-methylpyridazine 
• 98-80-6 phenylboronic acid 
• 103-79-7 1-phenyl-acetone 
• 105537-53-9 4-phenyl-5-methyl-5-hydroxy-2(5H)-furanone 

Downstream Products

• 105537-98-2 3-amino-5-phenyl-6-methylpyridazine 
• 105537-67-5 6-Amino-1-(3-carboxy-propyl)-3-methyl-4-phenyl-pyridazin-1-ium; bromide 
• 105538-15-6 6-Amino-1-(3-ethoxycarbonyl-propyl)-3-methyl-4-phenyl-pyridazin-1-ium; bromide 
• 140149-38-8 (6-Methyl-5-phenyl-pyridazin-3-yl)-hydrazine 

Relevant academic research and scientific papers

Ligand-dependent site-selective suzuki cross-coupling of 3,5-dichloropyridazines

General methods for the highly site-selective Suzuki monocoupling of 3,5-dichloropyridazines have been discovered. By changing the ligand employed, the preferred coupling site can be switched from the 3-position to the 5-position, typically considered the less reactive C-X bond. These conditions are applicable to the coupling of a wide variety of aryl-, heteroaryl-, and vinylboronic acids with high selectivities, thus enabling the rapid construction of diverse arrays of diarylpyradazines in a modular fashion.

Synthesis and Structure-Activity Relationships of Series of Aminopyridazine Derivatives of γ-Aminobutyric Acid Acting as Selective GABA-A Antagonists

We have recently shown that an aryloaminopyridazine derivarive of GABA, SR 95103 , is a selective and competitive GABA-A receptor antagonist.In order to further explore the structural requirements for GABA receptor affinity, we synthesized a series of 38 compounds by attaching various pyridazinic structures to GABA or GABA-like side chains.Most of the compounds displaced GABA from rat brain membranes.All the active compounds antagonized the GABA-elicited enhancement of diazepam binding, strongly suggesting that all these compounds are GABA-A receptor antagonists.None of the compounds that displaced GABA from rat brain membranes interacted with other GABA recognition sites (GABA-B receptor, GABA uptake binding site, glutamate decarboxylase, GABA-transaminase).They did not interact with the Cl- ionophore associated with the GABA-A receptor and did not interact with the benzodiazepine, strychnine, and glutamate binding sites.Thus these compounds appear to be specific GABA-A receptor antagonists.In terms of structure-activity, it can be concluded that a GABA moiety bearing a positive charge is necessary for optimal GABA-A receptor recognition.Additional binding sites are tolerated only if they are part of a charge-delocalized amidinic or guanidinic system.If this delocalization is achieved by linking a butyric acid moiety to the N(2) nitrogen of a 3-aminopyridazine, GABA-antagonistic character is produced.The highest potency (ca.250 times bicuculline) was observed when an aromatic ? system, bearing electron-donating substituents, was present on the 6-position of the pyridazine ring.