Issue 8, 2014

Interaction of oxovanadium(iv)–salphen complexes with bovine serum albumin and their cytotoxicity against cancer

Abstract

Vanadyl compounds of clinical significance are recommended as drugs against diseases such as tuberculosis, diabetes, cancer, etc. In order to check the potential of the salphen ligands and oxovanadium(IV)–salphen complexes as drugs their binding with bovine serum albumin (BSA) is investigated. The binding constants measured at pH 7.4 using UV-vis absorption and fluorescence techniques are in the range of 103–105 M−1. The quenching of the fluorescence of BSA and appearance of enhanced luminescence of the salphen ligand/vanadium(IV) complex at the increased [quencher] show efficient FRET from the protein to the quencher and the distance of energy transfer estimated using Forster's theory is in the range of 1.4–3.5 nm. Molecular docking studies (DFT) utilizing oxovanadium(IV)–salphen derivatives show strong binding with BSA and give insight into the binding modes, interaction pattern and stability of synthesized complexes in the target site. The cytotoxicity study shows the ability of these V(IV) complexes to inhibit the growth of AGS gastric cell lines.

Graphical abstract: Interaction of oxovanadium(iv)–salphen complexes with bovine serum albumin and their cytotoxicity against cancer

Supplementary files

Article information

Article type
Paper
Submitted
12 Sep 2013
Accepted
27 Nov 2013
First published
28 Nov 2013

Dalton Trans., 2014,43, 3260-3272

Author version available

Interaction of oxovanadium(IV)–salphen complexes with bovine serum albumin and their cytotoxicity against cancer

V. Gomathi Sankareswari, D. Vinod, A. Mahalakshmi, M. Alamelu, G. Kumaresan, R. Ramaraj and S. Rajagopal, Dalton Trans., 2014, 43, 3260 DOI: 10.1039/C3DT52505H

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