© 2019 Elsevier Inc. A series of eight hexacoordinated mixed-ligand oxidovanadium(IV) complexes [VO(Lx)(LN-N)] (1–8), where Lx = L1 – L4 are four differently substituted ONO donor aroylhydrazone ligands and LN-N are N,N-donor bases like 2,2′-bipyridine (bipy) (1, 3, 5 and 7) and 1,10-phenanthroline (phen) (2, 4, 6 and 8), have been reported. All synthesized complexes have been characterized by various physicochemical techniques and molecular structures of 1 and 6 were determined by X–ray crystallography. With a view to evaluate the biological activity of the VIVO species, the behavior of the systems VIVO2+/Lx, VIVO2+/Lx/bipy and VIVO2+/Lx/phen was studied as a function of pH in a mixture of H2O/DMSO 50/50 (v/v). DFT calculations allowed finding out the relative stability of the tautomeric forms of the ligands, and predicting the structure of vanadium complexes and their EPR parameters. To study their interaction with proteins, firstly the ternary systems VIVO2+/L1,2 with 1-methylimidazole, which is a good model for histidine binding, were examined. Subsequently the interaction of the complexes with lysozyme (Lyz), cytochrome c (Cyt) and bovine serum albumin (BSA) was studied. The results indicate that the complexes showed moderate binding affinity towards BSA, while no interaction takes place with lysozyme and cytochrome c. This could be explained with the higher number of accessible coordinating and polar residues for BSA than for Lyz and Cyt. Further, the complexes were also evaluated for their DNA binding propensity through UV–vis absorption titration and fluorescence spectral studies. These results were consistent with BSA binding affinity and showed moderate binding affinity towards CT-DNA.
- DFT calculations
- DNA binding
- Mixed-ligand oxidovanadium(IV)
- Protein interaction