The influence of pH and ionic strength on the interactions between human serum albumin and magnetic iron oxide nanoparticles

Human serum albumin (HSA) is a very well-characterized protein, which has already been used for many biocompatible coatings. We hypothesized binding between HSA and magnetic iron oxide nanoparticles (MNPs) as well as HSA coating stability to be pH- and ionic strength-dependent. The impact of phosphate buffer on protein coating was studied at varying pH (6.0, 6.6, and 7.5) and ionic strengths (0.15 and 0.30 M NaCl) using different physicochemical methods. In addition, the stability of HSA coatings on MNPs was studied by means of UV/visible spectrophotometry, dynamic light scattering, and electron magnetic resonance. We used differential scanning calorimetry (DSC) to determine the differences in the change of enthalpies and denaturation temperatures of HSA in various buffer conditions and on the surface of the particles. The binding thermodynamics of HSA and MNPs were determined by isothermal titration calorimetry (ITC), and it was also dependent on pH and ionic strength. The stability of adsorbed layer on MNPs decreases with increasing pH [from weakly acidic (pH 6.0–6.6) to slightly alkaline (pH 7.5)], as well as with an increase of ionic strength. This study develops stable HSA coating on MNPs which might be applied to a wide range of biomedical applications. [Display omitted] •Thermodynamic parameters of HSA change due to HSA interactions with MNPs.•Binding constants and stoichiometry of HSA association with MNPs are evaluated.•Stability of HSA coating on MNPs depends on pH and ionic strength of the buffer.•Immunoglobulin G helps to check HSA coating stability on MNPs surface.