7470-51-1

Usage

InChI:InChI=1/C11H13NO2/c1-3-11(14)12-10-6-4-9(5-7-10)8(2)13/h4-7H,3H2,1-2H3,(H,12,14)

Upstream product

• 591-50-4 iodobenzene 
• 22535-53-1 N-(4-acetylphenyl)-2-propenamide 
• 79-03-8 propionyl chloride 
• 99-92-3 p-aminobenzophenone 

Relevant academic research and scientific papers

Catalytic α-Hydroarylation of Acrylates and Acrylamides via an Interrupted Hydrodehalogenation Reaction

The palladium-catalyzed, α-selective hydroarylation of acrylates and acrylamides is reported. Under optimized conditions, this method is highly tolerant of a wide range of substrates including those with base sensitive functional groups and/or multiple enolizable carbonyl groups. A detailed mechanistic study was undertaken, and the high selectivity of this transformation was shown to be enabled by the formation of a [PdII(Ar)(H)] intermediate, which performs selective hydride insertion into the β-position of α,β-unsaturated carbonyl compounds.

Structure-based modification of 3-/4-aminoacetophenones giving a profound change of activity on tyrosinase: From potent activators to highly efficient inhibitors

In this study, we developed 3-/4-aminoacetophenones and their structure-based 3-/4-aminophenylethylidenethiosemicarbazide derivatives, respectively, as novel tyrosinase activators and inhibitors. Notably, all the obtained thiosemicarbazones displayed more potent tyrosinase inhibitory activities than kojic acid. Especially, compound 7k was found to be the most active tyrosinase inhibitor with IC50 value of 0.291 1/4M. The structure-activity relationships (SARs) analysis showed that: (1) the amine group was absolutely necessarily for determining the tyrosinase activation activity; (2) the introduction of thiosemicarbazide group played a very vital role in transforming tyrosinase activators into tyrosinase inhibitors; (3) the phenylethylenethiosemicarbazide moiety was crucial for determining the tyrosinase inhibitory activity; (4) the type of acyl group had no obvious effect on the inhibitory activity; (5) the position of amide substituent on the phenyl ring influenced the tyrosinase inhibitory potency. Moreover, the inhibition mechanism and inhibition kinetics study revealed that compound 7k was reversible and non-competitive inhibitor, and compound 8h was reversible and competitive-uncompetitive mixed-II type inhibitor.