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

Journal of fluorescence

PubMedID: 26139532

Mathavan A, Ramdass A, Rajagopal S. A Spectroscopy Approach for the Study of the Interaction of Oxovanadium(IV)-Salen Complexes with Proteins. J Fluoresc. 2015;.
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 a-helicity in the proteins. Docking studies indicate that mode of binding of oxovanadium(IV)-salen complexes with proteins is hydrophobic in nature.