25515-48-4

Upstream product

• 103826-24-0 (E)-3-(3,4-Dimethoxy-phenyl)-acrylic acid 3,5-dihydroxy-phenyl ester 
• 480-66-0 2,4,6-trihydroxyacetophenone 
• 120-14-9 3,4-dimethoxy-benzaldehyde 
• 65490-09-7 2'-hydroxy-4',6'-bis(methoxymethoxy)acetophenone 
• 188842-24-2 2'-hydroxy-3,4-dimethoxy-4',6'-bis(methoxymethoxy)chalcone 

Relevant academic research and scientific papers

Synthesis and Biological Evaluation of 2,4,6-Trihydroxychalcone Derivatives as Novel Protein Tyrosine Phosphatase 1B Inhibitors

A series of 2,4,6-trihydroxychalcone derivatives were synthesized and identified as reversible and competitive protein tyrosine phosphatase (PTP) 1B inhibitors with IC50 values in the micromolar range. Compound 4a had the greatest in vitro inhibition activity against PTP1B (IC50=0.27± 0.01μm) and the best selectivity (6.9-fold) for PTP1B relative to T-cell protein tyrosine phosphatases. The compounds identified herein provide a foundation on which to design specific inhibitors of PTP1B and other PTPs.

Synthesis and evaluation of 2′,4′,6′-trihydroxychalcones as a new class of tyrosinase inhibitors

In this study, we synthesized a series of hydroxychalcones and examined their tyrosinase inhibitory activity. The results showed that 2′,4′,6′-trihydroxychalcone (1), 2,2′,3,4′,6′-pentahydroxychalcone (4), 2′,3,4,4′,5,6′-hexahydroxychalcone (5), 2′,4′,6′-trihydroxy- 3,4-dimethoxychalcone (9) and 2,2′,4,4′,6′-pentahydroxychalcone (15) exhibited high inhibitory effects on tyrosinase with respect to l-tyrosine as a substrate. By the structure-activity relationship study, it was suggested that the 2′,4′,6′-trihydroxyl substructure in the chalcone skeleton were efficacious for the inhibition of tyrosinase activity. And also, the catechol structure on B-ring of chalcones was not advantageous for the inhibitory potency. Furthermore, 15 (IC50 = 1 μM) was found to show the highest activity out of a set of 15 hydroxychalcones, even better than both 2,2′,4,4′-tetrahydroxychalcone (13, IC50 = 5 μM) and kojic acid (16, IC50 = 12 μM), which were known as potent tyrosinase inhibitors. Kinetic study revealed that 15 acts as a competitive inhibitor of tyrosinase with Ki value of 3.1 μM.

Synthesis and evaluation of antiplatelet activity of trihydroxychalcone derivatives

In an effort to develop potent antiplatelet agents, a series of trihydroxychalcones was synthesized and screened in vitro for their inhibitory effects on washed rabbit platelet aggregation induced by arachidonic acid (100 μM) and collagen (10 μg/ml). Of five compounds with potent inhibitory effects on arachidonic acid- and collagen-induced platelet aggregation, compound 4e was found to be the most potent. The structure-activity relationships suggested that antiplatelet activity was governed to a greater extent by the substituent on B ring of the chalcone template, and most of the active compounds had methoxy or dimethoxy groups on B ring.

PHOTOREARRANGEMENT OF PHENYL CINNAMATES UNDER MICELLAR ENVIRONMENT

Photolysis of phenyl cinnamates in aqueous SDS medium results in an efficient and high yield synthesis of the corresponding 2'-hydroxychalcones.