4.6 Article

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

Journal

JOURNAL OF INORGANIC BIOCHEMISTRY
Volume 224, Issue -, Pages -

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2021.111582

Keywords

Salan; Mono-and dinuclear vanadium(V); Solution chemistry; Protein interaction; Cytotoxicity

Funding

  1. [01 (2963) /18/EMR-II]

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Three ONNO donor tetradentate diamino bis(phenolato) salan ligands were synthesized and used to form vanadium complexes, which were characterized and evaluated through various analyses including structural determination, electrochemical behavior, protein interaction studies, and cytotoxicity assessments against cancer and normal cell lines. The cytotoxicity trend of the complexes correlates with their protein binding affinity.
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-ethane (H2L2) and N, N '-bis-(5-chloro-2-hydroxy-3-isopropyl-6-methyl-benzyl)-1,2-diaminocyclohexane (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.

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