Antimetastatic effects and bioavailability studies of silibinin with oxidovanadium(IV) cation (VOsil)

NASO, LUCIANA G.; FERRER E.G; P.A.M. WILLIAMS

Buenos Aires-online

Encuentro; ANNUAL MEETING OF BIOSCIENCE SOCIETIES 2020; 2020

Fundación Revista Medicina

Objective: The flavolignan silibinin is the main component of silymarin. It has powerful anticancer and antimetastatic effects against malignant cell lines. In recent years, a great effort has been dedicated to the development of more effective and less toxic chemotherapeutic agents. In this sense, we evaluated the anticancer and antimetastatic activity on A549 cell line of silibinin and the complex VOsil, previously synthesized y characterized. Likewise, the ability of bovine serum albumin (BSA) to bind the compound was evaluated.Methods: The effect of silibinin and VOsil on the human lung cancer cell line (A549) viability was measured (MTT assay). In addition, the effect of the compounds at non-cytotoxic concentrations (5 µM) on adhesion, migration and invasion was investigated. On the other hand, the interaction between both compounds and BSA was investigated using tryptophan fluorescence quenching.Results: VOsil behaved as a more cytotoxic agent than the ligand at concentration 100 µM inhibiting 40 % of cell viability. The adhesion to fibronectin ability of cells treated with silibinin and VOsil decreased 34 and 58 %, respectively in comparison with the control. The number of migrating cells decreased about 50 % after VOsil treatment. Silibinin attenuated cell migration to a lesser extent (25%). A 40% and 23% reduction on cell invasion was observed when cells were treated with VOsil and silibinin, respectively. Usually, the oxidovanadium(IV) cation was less effective in all assays. Binding constant values for the interaction of silibinin (9.88 ± 0.95 x 106 L.mol-1) and VOsil (12.58 ± 0.76 x106 L.mol-1) with BSA were determined, suggesting high affinity of the compounds toward the protein. Also, n values of 1.07 ± 0.06 (silibinin) and 1.48 ± 0.07 (VOsil) were obtained indicating an interaction with one binding site of BSA. Conclusion: This study shows that the complexation enhances the biological effects of the free flavolignan.