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Insights into the binding interaction between copper ferrite nanoparticles and bovine serum albumin: An effect on protein conformation and activity
Author(s) -
Millan Sabera,
Kumar Aniket,
Satish Lakkoji,
Susrisweta B.,
Dash Priyabrat,
Sahoo Harekrushna
Publication year - 2018
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.3499
Subject(s) - circular dichroism , bovine serum albumin , chemistry , hydrogen bond , quenching (fluorescence) , enthalpy , protein secondary structure , copper , denaturation (fissile materials) , van der waals force , hydrophobic effect , crystallography , fourier transform infrared spectroscopy , fluorescence , nuclear chemistry , chromatography , molecule , organic chemistry , biochemistry , thermodynamics , chemical engineering , physics , quantum mechanics , engineering
The binding affinity between bovine serum albumin (BSA) and copper ferrite (CuFe 2 O 4 ) nanoparticles in terms of conformation, stability and activity of protein was studied using various spectroscopic methods. The quenching involved in BSA–CuFe 2 O 4 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 CuFe 2 O 4 NP. Furthermore, thermal denaturation observations were consistent with the circular dichroism results. The interaction of CuFe 2 O 4 NP with BSA decreased the esterase activity in the BSA assay, revealing the affinity of copper ferrite towards the active site of BSA.