54108-26-8Relevant articles and documents
Synthesis, in-vitro evaluation, molecular docking, and kinetic studies of pyridazine-triazole hybrid system as novel α-glucosidase inhibitors
Moghimi, Setareh,Salarinejad, Somayeh,Toolabi, Mahsa,Firoozpour, Loghman,Esmaeil Sadat Ebrahimi, Seyed,Safari, Fatemeh,Madani-Qamsari, Fatemeh,Mojtabavi, Somayeh,Faramarzi, Mohammad Ali,Karima, Saeed,Pakrad, Roya,Foroumadi, Alireza
, (2021/02/16)
In this study, we reported the discovery of pyridazine based 1,2,3-triazole derivatives as inhibitors of α-glucosidase. All target compounds exhibited significant inhibitory activities against yeast and rat α-glucosidase enzymes compared to positive control, acarbose. The most potent compound 6j, ethyl 3-(2-(1-(4-nitrobenzyl)-1H-1,2,3-triazol-4-yl)ethyl)-5,6-diphenylpyridazine-4-carboxylate exhibited IC50 values of 58, and 73 μM. Docking studies indicated the responsibility of hydrophobic and hydrogen bonding interactions in the ligand-enzyme complex stability. The in-vitro safety against the normal cell line was observed by toxicity evaluation of the selected compounds.
Design and synthesis of novel pyridazine N-aryl acetamides: In-vitro evaluation of α-glucosidase inhibition, docking, and kinetic studies
Faramarzi, Mohammad Ali,Firoozpour, Loghman,Foroumadi, Alireza,Moghimi, Setareh,Mojtabavi, Somayeh,Sadat Ebrahimi, Seyed Esmaeil,Safari, Fatemeh,Salarinejad, Somayeh,Toolabi, Mahsa
, (2020/07/21)
We herein applied the four step-synthetic route to prepare the pyridazine core attached to the various N-aryl acetamides. By this approach, a new series of pyridazine-based compounds were synthesized, characterized and evaluated for their activities against α-glucosidase enzyme. In-vitro α-glucosidase assay established that twelve compounds are more potent than acarbose. Compound 7a inhibited α-glucosidase with the IC50 value of 70.1 μM. The most potent compounds showed no cytotoxicity against HDF cell line. Molecular docking and kinetic studies were performed to determine the modes of interaction and inhibition, respectively.