520-28-5Relevant articles and documents
Ruthenium(II) trithiacyclononane complexes of 7,3′,4′-trihydroxyflavone, chrysin and tectochrysin: Synthesis, characterisation, and cytotoxic evaluation
Marques, Joana,Silva, Artur M.S.,Marques, Maria Paula M.,Braga, Susana S.
, p. 71 - 79 (2019)
This study describes a simple, two-step method for obtaining ruthenium(II) trithiacyclononane ([9]aneS3) flavonate complexes in yields ranging from 23% to 34%. With 7,3′,4′-trihydroxyflavone (thflv), a neutral complex, [Ru(II)([9]aneS3)(DMSO)(thflv)] (1), is formed by coordination at the catechol group. With chrysin (chrys) and tectochrysin (tchrys), Ru(II) binds to the chromenone fragment to form cationic complexes that are isolated as [Ru(II)([9]aneS3)(chrys)(DMSO)]Cl (2) and [Ru(II)([9]aneS3)(DMSO)(tchrys)]Cl (3). The structure of the complexes is characterised by FT-IR, NMR and ESI+-MS. Furthermore, the flavones and the corresponding complexes, 1–3, were investigated regarding their in vitro cytotoxic activity towards four different human tumour cell lines, PC-3 (prostate), MG-63 (osteosarcoma), MCF-7 and MDA-MB-231 (both breast adenocarcinoma).
Correlation study on methoxylation pattern of flavonoids and their heme-targeted antiplasmodial activity
Boutefnouchet, Sabrina,Bouzidi, Chouaha,Cojean, Sandrine,Figadère, Bruno,Grougnet, Rapha?l,Maciuk, Alexandre,Michel, Sylvie,Ortiz, Sergio,Vásquez-Ocmín, Pedro G.
, (2020/09/16)
A library of 33 polymethoxylated flavones (PMF) was evaluated for heme-binding affinity by biomimetic MS assay and in vitro antiplasmodial activity on two strains of P. falciparum. Stability of heme adducts was discussed using the dissociation voltage at 50% (DV50). No correlation was observed between the methoxylation pattern and the antiparasitic activity, either for the 3D7 chloroquine-sensitive or for the W2 chloroquine-resistant P. falciparum strains. However, in each PMF family an increased DV50 was observed for the derivatives methoxylated in position 5. Measurement of intra-erythrocytic hemozoin formation of selected derivatives was performed and hemozoin concentration was inversely correlated with heme-binding affinity. Kaempferol showed no influence on hemozoin formation, reinforcing the hypothesis that this compound may exert in vitro antiplasmodial activity mostly through other pathways. Pentamethoxyquercetin has simultaneously demonstrated a significant biological activity and a strong interaction with heme, suggesting that inhibition of hemozoin formation is totally or partially responsible for its antiparasitic effect.
New alkoxy flavone derivatives targeting caspases: Synthesis and antitumor activity evaluation
Moreira, Joana,Ribeiro, Diana,Silva, Patrícia M. A.,Nazareth, Nair,Monteiro, Madalena,Palmeira, Andreia,Saraiva, Lucília,Pinto, Madalena,Bousbaa, Hassan,Cidade, Honorina
, (2019/01/14)
The antitumor activity of natural flavonoids has been exhaustively reported. Previously it has been demonstrated that prenylation of flavonoids allows the discovery of new compounds with improved antitumor activity through the activation of caspase-7 activity. The synthesis of twenty-five flavonoids (4-28) with one or more alkyl side chains was carried out. The synthetic approach was based on the reaction with alkyl halide in alkaline medium by microwave (MW) irradiation. The in vitro cell growth inhibitory activity of synthesized compounds was investigated in three human tumor cell lines. Among the tested compounds, derivatives 6, 7, 9, 11, 13, 15, 17, and 18 revealed potent growth inhibitory activity (GI50 10 μM), being the growth inhibitory effect of compound 13 related with a pronounced caspase-7 activation on MCF-7 breast cancer cells and yeasts expressing human caspase-7. A quantitative structure-activity relationship (QSAR) model predicted that hydrophilicity, pattern of ring substitution/shape, and presence of partial negative charged atoms were the descriptors implied in the growth inhibitory effect of synthesized compounds. Docking studies on procaspase-7 allowed predicting the binding of compound 13 to the allosteric site of procaspase-7.
