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

LUCIANA G. NASO; EVELINA G FERRER; PATRICIA A. M. WILLIAMS

Buenos Aires-online

Encuentro; ANNUAL MEETING OF BIOSCIENCE SOCIETIES 2020; 2020

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 therapeutic agents. In this sense, we evaluated the anticancer and antimetastatic activity on A549 cell line of silibinin and the complexVOsil, previously synthesized and 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 atconcentration 100 μM inhibiting 40 % of cell viability. The adhesion tofibronectin ability of cells treated with silibinin and VOsil decreased34 and 58 %, respectively in comparison with the control. The numberof 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 weretreated with VOsil and silibinin, respectively. Usually, the oxidovanadium(IV) cation was less effective in all assays. Binding constantvalues for the interaction of silibinin (9.88 ± 0.95 x 106 L.mol-1) andVOsil (12.58 ± 0.76 x106 L.mol-1) with BSA were determined, suggestinghigh affinity of the compounds toward the protein. Also, nvalues of 1.07 ± 0.06 (silibinin) and 1.48 ± 0.07 (VOsil) were obtainedindicating an interaction with one binding site of BSA.Conclusion: This study shows that the complexation enhances thebiological effects of the free flavolignan.