In the past decade, profuse research efforts explored the uses of iron oxide particles in nanomedicine. To a great extent, the efficiency and fate of those magnetic nanoparticles depend on how their surfaces interface with the proteins in a physiological environment. It is well reported how an ungoverned protein corona can be detrimental to cellular uptake and targeting efficiency and how it can modify the nanoparticles biodistribution. Novel strategies are emerging to achieve enhanced and more reproducible performances of engineered nanoparticles with a custom-built protein corona. Here we report on a generalized protocol to preform a monolayer of human serum albumin (HSA) on superparamagnetic iron oxide nanoparticles (SPIONs) of different sizes. The resulting molecular structures are described by molecular dynamics simulations of the hybrid nanoconjugates. The simulations outcomes regarding the number of proteins in the corona and their monolayer arrangement on the particle surface are in agreement with the results obtained from dynamic light scattering and electronic microscopy analysis. Using tryptophan fluorescence quenching, we revealed the existence of a strong interaction between the SPIONs and the HSA which endorses the robustness of the protein-nanoparticle conjugates in this system. Moreover, we evaluated the effect of the HSA corona on the SPIONs efficiency as magnetic resonance imaging (MRI) contrast agents in water, human serum, and saline media. The protein corona did not affect the efficiency of the SPIONs as T2 contrast agents but reduce their T1 efficiency. In addition, we observed a greater stability for HSA-SPIONs nanoconjugates in saline and in acid media, preventing nanoparticle dissolution in extreme gastric conditions.
Keywords: albumin corona; human serum albumin; magnetic resonance imaging; metabolization; superparamagnetic iron oxide nanoparticles.