PHYSICO-CHEMICAL PROPERTIES INTERACTION OF NICKEL NANOCOMPLEX WITH BOVIN SERUM ALBUMIN TO CANCER TREATMENTS

Since the properties of materials change as their size approaches the nanoscale and as the percentage of atoms at the surface of a material becomes significant, in this study, we report the interaction between Ni(II) nanocomplex with bovine serum albumin (BSA) in detailed using fluorescence spectroscopy, UV-Via absorption, circular dichroism spectroscopy. We report the quenching mechanism, binding mode, binding constant (Kb), number of binding sites and the apparent distance between donor and acceptor. The enhancement of the interaction studies indicated that the mechanism of quenching is dynamic and that hydrophobic force plays a major role in stabilizing BSA–Ni(II) complex with binding constant of 104 M-1. The results of synchronous fluorescence, 3D fluorescence, UV–Vis absorption, and CD spectra indicated that the microenvironment and the secondary structure of BSA are altered in the presence of Ni(II) complex. In addition, the binding studies between this complex and BSA give us key insights into the transportation, distribution and toxicity of newly design antitumor complexes in blood.