Abstract
Oxovanadium(IV)-salen complexes bind with bovine serum albumin (BSA) and ovalbumin (OVA) strongly with binding constant in the range 104–107 M−1 at physiological pH (7.4) confirmed using UV–visible absorption, fluorescence spectral and circular dichroism (CD) study. CD results show that the binding of oxovanadium(IV) complexes induces the conformational change with the loss of α-helicity in the proteins. Docking studies indicate that mode of binding of oxovanadium(IV)-salen complexes with proteins is hydrophobic in nature.
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Prof. S.R thanks UGC, New Delhi for sanctioning UGC-BSR Faculty and UGC Emeritus Fellowships. AM thanks the UGC, New Delhi and the Management of V. O. C. College, Tuticorin for sanctioning permission to avail the benefits of Faculty Development Programme (FDP). A.R is the recipient of UGC Meritorious fellowship under the Basic Scientific Research (BSR) Scheme.
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Mathavan, A., Ramdass, A. & Rajagopal, S. A Spectroscopy Approach for the Study of the Interaction of Oxovanadium(IV)-Salen Complexes with Proteins. J Fluoresc 25, 1141–1149 (2015). https://doi.org/10.1007/s10895-015-1604-3
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DOI: https://doi.org/10.1007/s10895-015-1604-3