Chemistry of mixed-ligand oxidovanadium(IV) complexes of aroylhydrazones incorporating quinoline derivatives: Study of solution behavior, theoretical evaluation and protein/DNA interaction

Autor(en): Banerjee, Atanu
Dash, Subhashree P.
Mohanty, Monalisa
Sanna, Daniele
Sciortino, Giuseppe
Ugone, Valeria
Garribba, Eugenio
Reuter, Hans 
Kaminsky, Werner
Dinda, Rupam
Stichwörter: (VO)-O-IV COMPLEXES; Aroylhydrazone; Biochemistry & Molecular Biology; BLOOD-PLASMA; Chemistry; Chemistry, Inorganic & Nuclear; DFT calculations; DNA binding; HYPERFINE COUPLING-CONSTANTS; IN-VITRO; INSULIN-MIMETIC ACTIVITY; Mixed-ligand oxidovanadium(IV); NON-OXIDO VANADIUM(IV); PHOTOINDUCED DNA CLEAVAGE; Protein interaction; SPECTROSCOPIC CHARACTERIZATION; TRANSITION-METAL-COMPLEXES; VANADYL COMPLEXES
Erscheinungsdatum: 2019
Herausgeber: ELSEVIER SCIENCE INC
Enthalten in: JOURNAL OF INORGANIC BIOCHEMISTRY
Band: 199
Zusammenfassung: 
A series of eight hexacoordinated mixed-ligand oxidovanadium(IV) complexes [VO(L-x)(LN-N)] (1-8), where L-x = L-1 - L-4 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 (VO)-O-IV species, the behavior of the systems (VO2+)-O-IV/L-x, (VO2+)-O-IV/L-x/bipy and (VO2+)-O-IV/L-x/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 (VO2+)-O-IV/L-1,L-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.
ISSN: 01620134
DOI: 10.1016/j.jinorgbio.2019.110786

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