Influence of pH on interaction of silver nanoparticles - protein: Analyses by spectroscopic and thermodynamic ideology

Abstract

To investigate the interaction between bovine serum albumin (BSA) and silver nanoparticles (AgNPs) at five different pHs (below (3.0 and 4.0), above (7.4 and 9.2) and at the isoelectric point (4.7) of BSA) by spectroscopic (viz., UV–vis, fluorescence, circular dichroism (CD)), microscopic (viz., atomic force microscopy (AFM), transmission electron microscopy (TEM), field emission scanning electron microscope (FESEM)) and thermodynamic (viz., isothermal titration calorimetry (ITC)) methods. The fluorescence quenching spectra provided binding constants via Stern-Volmer plot, quenching constant (Ksv) and rate constant (Kq) were calculated. From the CD spectra, it is clear that the α-helix decreases by increasing the AgNP’s concentration. However, at isoelectric point (pH = 4.7), BSA shows more helicity in the presence of AgNPs, which indicates that the structures of BSA become more ordered and stable, and aggregation occurs at strong acidic (3.0), and basic medium (9.2) Fluorescence spectra also indicate the aggregation of the protein at strong acidic (pH = 3.0) and basic medium (pH = 9.2). Furthermore, the morphological and topographical evolute ion upon the interaction was examined using TEM, FESEM, and AFM. The studies conclude the effect of the pH in the medium and behavior of AgNPs with BSA by using different spectroscopic and microscopic techniques.