949580-62-5

Upstream product

• 672-13-9 2-hydroxy-5-methoxybenzaldehyde 
• 25307-01-1 p-tolylacetic acid sodium salt 
• 622-47-9 4-tolylacetic acid 
• 351981-21-0 C₁₅H₁₆N₂O₄S 
• 766-97-2 4-n-methylphenylacetylene 

Downstream Products

• 949580-75-0 3-(4-bromomethylphenyl)-6-methoxychromen-2-one 
• 1338596-71-6 6-hydroxy-3-(4-methylphenyl)coumarin 
• 1338596-72-7 3-(4′-methylphenyl)-6-(2-oxopropoxy)coumarin 
• 1338596-73-8 6-(2-cyclopentyloxy)-3-(4-methylphenyl)coumarin 

Relevant academic research and scientific papers

Visible-light-driven copper-catalyzed aerobic oxidative cascade cyclization of N-tosylhydrazones and terminal alkynes: Regioselective synthesis of 3-arylcoumarins

We present the first example of sustainable, intuitive, highly regioselective, visible-light-driven copper catalyzed aerobic oxidative cascade cyclization of N-tosylhydrazones with terminal alkynes for the preparation of 3-arylcoumarins at room temperature. This operationally simple methodology has been successfully applied to a wide range of N-tosylhydrazones and alkynes (49 examples), and proceeds well to afford biologically active compounds, such as monoamine oxidase B (MAO-B) inhibitor and horseradish peroxidase (HRP) inhibitor, in satisfactory yields under mild conditions. Furthermore, mechanistic studies suggest that the reaction proceeds via a copper(ii)-superoxo or -peroxo complex mediated oxidative annulation of terminal alkynes, as evidenced by 18O2 isotopic-labelling experiments.

Synthesis and study of a series of 3-arylcoumarins as potent and selective monoamine oxidase B inhibitors

New series of 6-substituted-3-arylcoumarins displaying several alkyl, hydroxyl, halogen, and alkoxy groups in the two benzene rings have been designed, synthesized, and evaluated in vitro as human monoamine oxidase A and B (hMAO-A and hMAO-B) inhibitors.

Extensive SAR and computational studies of 3-{4-[(benzylmethylamino)methyl] phenyl}-6,7-dimethoxy-2H-2-chromenone (AP2238) derivatives

AP2238 was the first compound published to bind both anionic sites of the human acetylcholinesterase, allowing the simultaneous inhibition of the catalytic and the amyloid-β pro-aggregating activities of AChE. Here we attempted to derive a comprehensive structure-activity relationship picture for this molecule, affording 28 derivatives for which AChE and BChE inhibitory activities were evaluated. Selected compounds were also tested for their ability to prevent the AChE-induced Aβ-aggregation. Moreover, docking simulations and molecular orbital calculations were performed.