Protein binding and cytotoxic activities of monomeric and dimeric oxido-vanadium(V) salan complexes: Exploring the solution behavior of monoalkoxido-bound oxido-vanadium(V) complex

Autor(en): Patra, Sushree Aradhana
Mohanty, Monalisa
Banerjee, Atanu
Kesarwani, Shivani
Henkel, Felix
Reuter, Hans 
Dinda, Rupam
Stichwörter: ANTIDIABETIC VANADIUM COMPLEXES; Biochemistry & Molecular Biology; BIOLOGICAL-ACTIVITIES; BIS(4,7-DIMETHYL-1,10-PHENANTHROLINE) SULFATOOXOVANADIUM(IV); Chemistry; Chemistry, Inorganic & Nuclear; Cytotoxicity; DIOXIDOVANADIUM(V) COMPLEXES; HUMAN SERUM-ALBUMIN; IN-VITRO CYTOTOXICITY; MOLECULAR DOCKING; Mono-and dinuclear vanadium(V); MONOOXO-VANADIUM(V) COMPLEX; OXIDOVANADIUM(V) COMPLEXES; PHOTOINDUCED DNA CLEAVAGE; Protein interaction; Salan; Solution chemistry
Erscheinungsdatum: 2021
Herausgeber: ELSEVIER SCIENCE INC
Journal: JOURNAL OF INORGANIC BIOCHEMISTRY
Volumen: 224
Zusammenfassung: 
Three ONNO donor tetradentate diamino bis(phenolato) ``salan'' ligands, N, N `-dimethyl-N, N `-bis-(5-chloro-2-hydroxy-3-methyl-benzyl)-1,2-diaminoethane (H2L1), N, N `-dimethyl-N, N `-bis-(5-chloro-2-hydroxy-3-isopropyl-6-methyl-benzyl)-1,2-diamino-ethan e (H2L2) and N, N `-bis-(5-chloro-2-hydroxy-3-isopropyl-6-methyl-benzyl)-1,2-diaminocycloh exane (H2L3) have been synthesized by following Mannich condensation reaction. Reaction of these ligands with their corresponding vanadium metal precursors gave one oxidomethoxidovanadium(V) [(VOL1)-O-V(OCH3)] (1) and two monooxido-bridged divanadium (V, V) complexes [(VOL2-3)-O-V](2)(mu-O) (2-3). The complexes were characterized by IR, UV-vis, NMR and ESI mass spectrometry. Also, the structure of all the complexes (1-3) was confirmed by the Single-Crystal X-ray diffraction analysis, which revealed a distorted octahedral geometry around the metal centres. The solution behavior of the [(VOL1)-O-V(OCH3)] (1) reveals the formation of two different types of V(V) species in solution, the structurally characterized compound 1 and its corresponding monooxido-bridged divanadium (V, V) complex [(VOL1)-O-V](2)(mu-O), which was further studied by IR, and NMR spectroscopy. The electrochemical behavior of all the complexes was evaluated through cyclic voltammetry. Interaction of the salan-V(V) complexes with human serum albumin (HSA) and bovine serum albumin (BSA) were analysed through fluorescence quenching, UV-vis absorption titration, synchronous fluorescence, circular dichroism studies, and fo spacing diaeresis rster resonance energy transfer (FRET). Finally, the in vitro cytotoxicity of the complexes was investigated against MCF-7 and HT-29 and NIH-3T3 cell lines. Cytotoxicity value of complexes in both MCF-7 and HT-29 follows the same trend that is 3 > 1 > 2 which is in line with protein binding affinity of the complexes.
ISSN: 01620134
DOI: 10.1016/j.jinorgbio.2021.111582

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