949580-77-2

Upstream product

• 127073-91-0 3-(3′,4′-dimethoxyphenyl)-6-methylcoumarin 
• 613-84-3 2-hydroxy-5-methylbenzaldehyde 
• 106-44-5 p-cresol 
• 60075-23-2 3,4-dimethoxyphenylacetic acid hydrazide 

Downstream Products

• 1387531-39-6 trans-3-(3,4-dimethoxyphenyl)-6-styrylcoumarin 
• 1387531-40-9 cis-3-(3,4-dimethoxyphenyl)-6-(4-methoxystyryl)coumarin 
• 1387531-45-4 trans-3-(3,4-dimethoxyphenyl)-6-(4-methoxystyryl)coumarin 
• 1387531-46-5 cis-3-(3,4-dimethoxyphenyl)-6-(3,5-dimethoxystyryl)coumarin 
• 1387531-47-6 trans-3-(3,4-dimethoxyphenyl)-6-(3,5-dimethoxystyryl)coumarin 

Relevant academic research and scientific papers

Synthesis and biological evaluation of resveratrol-coumarin hybrid compounds as potential antitumor agents

Eighteen resveratrol-coumarin hybrid compounds (6 or 7-styryl-3- phenylcoumarin) were designed, synthesized and thirteen compounds were evaluated for their antitumor activities against MCF-7, HCT-28, and K562 tumor cell lines. Among them, compounds 2Z, 2E, 5E, and 7E showed varying degrees of growth inhibition of the above cell lines (IC50: 3.78-19.16 μmol/L). On the basis of the biological results, structure-activity relationships were obtained and discussed.

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.