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A Spectroscopy Approach for the Study of the Interaction of Oxovanadium(IV)-Salen Complexes with Proteins

Alagarsamy Mathavan1, Arumugam Ramdass, Seenivasan Rajagopal

  • 1Department of Chemistry, V. O. Chidambaram College, Tuticorin, 628 008, India.

Journal of Fluorescence
|July 4, 2015
PubMed

Oxovanadium(IV)-salen complexes bind with bovine serum albumin (BSA) and ovalbumin (OVA) strongly with binding constant in the range 10(4)-10(7) 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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