Insights into the binding interaction between copper ferrite nanoparticles and bovine serum albumin: An effect on protein conformation and activity

August 13, 2018

Title

Insights into the binding interaction between copper ferrite nanoparticles and bovine serum albumin: An effect on protein conformation and activity

Author

Sabera Millan, Aniket Kumar, Lakkoji Satish, B. Susrisweta, Priyabrat Dash, Harekrushna Sahoo

Year

2018

Journal

Luminescence

Abstract

The binding affinity between bovine serum albumin (BSA) and copper ferrite (CuFe2O4) nanoparticles in terms of conformation, stability and activity of protein was studied using various spectroscopic methods. The quenching involved in BSA–CuFe2O4 NP interaction was static quenching as analysed by different techniques (steady‐state and time‐resolved fluorescence along with temperature‐dependent fluorescence measurements). Among all types of possible interactions, it was revealed that the major binding forces were van der Waals interaction and hydrogen bonding, which were explored from negative values of enthalpy change (∆H = −193.85 kJ mol−1) and entropy change (∆S = −588.88 J mol−1 K−1). Additionally, synchronous, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy measurements confirmed the conformational changes in BSA upon the addition of CuFe2O4 NP. Furthermore, thermal denaturation observations were consistent with the circular dichroism results. The interaction of CuFe2O4 NP with BSA decreased the esterase activity in the BSA assay, revealing the affinity of copper ferrite towards the active site of BSA.

Instrument

J-1500

Keywords

Circular dichroism, Secondary structure, Ligand binding, Nanostructures, Materials, Biochemistry