22105-04-0Relevant articles and documents
Solvent-Controlled Hydrogenation of 2’-Hydroxychalcones: A Simple Solution to the Total Synthesis of Bussealins
Soto, Martín,Soengas, Raquel G.,Rodríguez-Solla, Humberto
, p. 5422 - 5431 (2020/10/06)
A solvent-controlled hydrogenation of 2’-hydroxychalcones to selectively obtain different hydrogenation products is herein reported. Thus, hydrogenation of 2’-hydroxychalcones using EtOH as solvent provided the corresponding 1,3-diarylpropanes in excellent yields. On the contrary, when the hydrogenation was performed in DCM, the corresponding dihydrochalcones were isolated. Switching the reaction solvent to n-BuOH/H2O (1:1), afforded 1,3-diarylpropanols from moderate to good yields. The methodology here reported offers a straightforward, simple and cost-effective method for the preparation of a wide variety of 2’-hydroxy-1,3-diarylpropanes derivatives, and was also applied to the preparation of natural Bussealins C and D. (Figure presented.).
Synthesis, activity and molecular modeling of a new series of chromones as low molecular weight protein tyrosine phosphatase inhibitors
Forghieri, Marco,Laggner, Christian,Paoli, Paolo,Langer, Thierry,Manao, Giampaolo,Camici, Guido,Bondioli, Lucia,Prati, Fabio,Costantino, Luca
experimental part, p. 2658 - 2672 (2009/09/08)
Protein tyrosine phosphatases (PTP) are crucial elements in eukaryotic signal transduction. Several reports suggested that the LMW-PTP family has oncogenic relevance. Moreover, LMW-PTP has been recognized as a negative regulator of insulin-mediated mitotic and metabolic signaling. Thus, inhibition of the LMW-PTP can be considered an attractive approach for the design of new therapeutic agents for the treatment of type II diabetes and for new antitumoral drugs. To date very few (and weak) inhibitors of LMW-PTP have been identified. On the basis of the reported weak activity of some flavonoids on phosphatases, we discovered a lead that originated a new class of highly active LMW-PTP inhibitors; these compounds inhibit also PTP-1B and are active in cellular assays. Docking experiments and SAR highlighted the possible binding mode of these compounds to the enzyme, putting the background for the future optimization of their inhibitory activity and selectivity towards the closely related enzyme PTP-1B.