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

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dc.contributor.authorPatra, Sushree Aradhana
dc.contributor.authorMohanty, Monalisa
dc.contributor.authorBanerjee, Atanu
dc.contributor.authorKesarwani, Shivani
dc.contributor.authorHenkel, Felix
dc.contributor.authorReuter, Hans
dc.contributor.authorDinda, Rupam
dc.date.accessioned2021-12-23T16:12:14Z-
dc.date.available2021-12-23T16:12:14Z-
dc.date.issued2021
dc.identifier.issn01620134
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/10111-
dc.description.abstractThree 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.
dc.description.sponsorship[01 (2963) /18/EMR-II]; The authors thank the reviewers for their comments and suggestions, which were helpful in preparing the revised version of the manuscript. R. D thanks CSIR, Govt. of India [Grant No. 01 (2963) /18/EMR-II] for funding this research.
dc.language.isoen
dc.publisherELSEVIER SCIENCE INC
dc.relation.ispartofJOURNAL OF INORGANIC BIOCHEMISTRY
dc.subjectANTIDIABETIC VANADIUM COMPLEXES
dc.subjectBiochemistry & Molecular Biology
dc.subjectBIOLOGICAL-ACTIVITIES
dc.subjectBIS(4,7-DIMETHYL-1,10-PHENANTHROLINE) SULFATOOXOVANADIUM(IV)
dc.subjectChemistry
dc.subjectChemistry, Inorganic & Nuclear
dc.subjectCytotoxicity
dc.subjectDIOXIDOVANADIUM(V) COMPLEXES
dc.subjectHUMAN SERUM-ALBUMIN
dc.subjectIN-VITRO CYTOTOXICITY
dc.subjectMOLECULAR DOCKING
dc.subjectMono-and dinuclear vanadium(V)
dc.subjectMONOOXO-VANADIUM(V) COMPLEX
dc.subjectOXIDOVANADIUM(V) COMPLEXES
dc.subjectPHOTOINDUCED DNA CLEAVAGE
dc.subjectProtein interaction
dc.subjectSalan
dc.subjectSolution chemistry
dc.titleProtein binding and cytotoxic activities of monomeric and dimeric oxido-vanadium(V) salan complexes: Exploring the solution behavior of monoalkoxido-bound oxido-vanadium(V) complex
dc.typejournal article
dc.identifier.doi10.1016/j.jinorgbio.2021.111582
dc.identifier.isiISI:000704265600008
dc.description.volume224
dc.identifier.eissn18733344
dc.publisher.placeSTE 800, 230 PARK AVE, NEW YORK, NY 10169 USA
dcterms.isPartOf.abbreviationJ. Inorg. Biochem.
crisitem.author.deptInstitut für Chemie neuer Materialien-
crisitem.author.deptidinstitute11-
crisitem.author.parentorgFB 05 - Biologie/Chemie-
crisitem.author.grandparentorgUniversität Osnabrück-
crisitem.author.netidReHa636-
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