دورية أكاديمية
Insights into the mechanisms underlying the antitumor activity of an oxidovanadium(IV) compound with the antioxidant naringenin. Albumin binding studies
| العنوان: | Insights into the mechanisms underlying the antitumor activity of an oxidovanadium(IV) compound with the antioxidant naringenin. Albumin binding studies |
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| المؤلفون: | Islas, María Soledad, Naso, Luciana Gissella, Lezama, Luis, Valcarcel, María, Salado, Clarisa, Roura Ferrer, Meritxell, Ferrer, Evelina Gloria, Williams, Patricia Ana María |
| بيانات النشر: | Elsevier Science Inc. |
| المجموعة: | CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
| مصطلحات موضوعية: | ANTIOXIDANT PROPERTIES, BSA BINDING, MECHANISM CYTOTOXIC ACTION, NARINGENIN, OXIDOVANADIUM(IV) COMPLEXES, https://purl.org/becyt/ford/1.4Test, https://purl.org/becyt/ford/1Test |
| الوصف: | Naringenin, a natural antioxidant present in grapefruit, oranges and the skin of tomatoes showed low antioxidant properties among other flavonoids due to its structural characteristics. Since many flavonoids were shown to have cell-killing and antioxidant activities, naringenin was investigated herein. In parallel with its antioxidant activities the flavonoid showed very low cytotoxicity at concentrations up to 100 μM against lung (A549) and breast (SKBr3 and MDAMB231) cancer cell lines. Furthermore, a newly-synthesized and characterized complex of naringenin and oxidovanadium(IV) ([VIVO(nar)2]·2H2O, VOnar, with weak ferromagnetic coupling) was also studied. As a result, VOnar acted as a better compound on cell-killing and antioxidant activities (in vitro) than naringenin. The anti-proliferative effect of VOnar was accompanied by reactive oxygen species (ROS) generation, cell membrane and DNA damages, cell cycle arrest, caspase 3/7 activation and mitochondrial potential reduction. The higher parameters observed for the MDAMB231 cell line have been related to its low glutathione (GSH) content. The assays of the interaction of bovine serum albumin (BSA) with the complex showed the affinity of protein toward it and that there is only one binding site on the BSA molecule. However, metal complexation decreased the binding affinity to BSA of naringenin probably due to a steric hindrance of the complex. ; Fil: Islas, María Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; Argentina ; Fil: Naso, Luciana Gissella. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. ... |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 0162-0134 |
| العلاقة: | info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0162013415001051Test; http://hdl.handle.net/11336/180846Test; Islas, María Soledad; Naso, Luciana Gissella; Lezama, Luis; Valcarcel, María; Salado, Clarisa; et al.; Insights into the mechanisms underlying the antitumor activity of an oxidovanadium(IV) compound with the antioxidant naringenin. Albumin binding studies; Elsevier Science Inc.; Journal of Inorganic Biochemistry; 149; 4-2015; 12-24; CONICET Digital; CONICET |
| الإتاحة: | https://doi.org/10.1016/j.jinorgbio.2015.04.011Test http://hdl.handle.net/11336/180846Test |
| حقوق: | info:eu-repo/semantics/openAccess ; https://creativecommons.org/licenses/by-nc-sa/2.5/arTest/ |
| رقم الانضمام: | edsbas.BEF8F6DD |
| قاعدة البيانات: | BASE |
| تدمد: | 01620134 |
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