4.6 Article

Bovine serum albumin binding, antioxidant and anticancer properties of an oxidovanadium(IV) complex with luteolin

期刊

JOURNAL OF INORGANIC BIOCHEMISTRY
卷 157, 期 -, 页码 80-93

出版社

ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2016.01.021

关键词

Luteolin; Oxidovanadium(IV) complexes; Magnetic properties; Mechanisms of cytotoxic action; BSA binding

资金

  1. UNLP
  2. CONICET
  3. CICPBA [PICyT 813/13]
  4. ANPCyT, Argentina [PICT-2013-0569]

向作者/读者索取更多资源

Chemotherapy using metal coordination compounds for cancer treatment is the work of the ongoing research. Continuing our research on the improvement of the anticancer activity of natural flavonoids by metal complexation, a coordination compound of the natural antioxidant flavone luteolin (lut) and the oxidovanadium(IV) cation has been synthesized and characterized. Using different physicochemical measurements some structural aspects of [VO(lut)(H2O)(2)]Na center dot 3H(2)O (VOlut) were determined. The metal coordinated to two cis-deprotonated oxygen atoms (ArO-) of the ligand and two H2O molecules. Magnetic measurements in solid state indicated the presence of an effective exchange pathway between adjacent vanadium ions. VOlut improved the antioxidant capacity of luteolin only against hydroxyl radical. The antitumoral effects were evaluated on MDAMB231 breast cancer and A549 lung cancer cell lines. VOlut exhibited higher viability inhibition (IC50 = 17 mu M) than the ligand on MDAMB231 cells but they have the same behavior on A549 cells (ca. IC50 = 60 mu M). At least oxidative stress processes were active during cancer cell-killing. When metals chelated through the carbonyl group and one adjacent OH group of the flavonoid an effective improvement of the biological properties has been observed. In VOlut the different coordination may be the cause of the small improvement of some of the tested properties of the flavonoid. Luteolin and VOlut could be distributed and transported in vivo. Luteolin interacted in the micro environment of the tryptophan group of the serum binding protein, BSA, by means of electrostatic forces and its complex bind the protein by H bonding and van der Waals interactions. (C) 2016 Elsevier Inc. All rights reserved.

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