Abstract

In a physiological fluid (e.g., blood), nanomaterials will strongly interact with proteins to form “protein corona”. The structure and aggregation of protein corona around the nanoparticles are of vital importance in the safe application of nanomaterials in living organisms. Here, we combined systematic methods, including transmission electron microscopy, scanning electron microscopy equipped with energy dispersive X-ray spectroscopy, Fourier transform infrared spectroscopy, hydrogen/deuterium exchange techniques and fluorescence quenching to explore the conformational change, stability and aggregation of protein corona bound on magnetic nanoparticles. For the first time we observed that the conformational change of protein corona could induce proteins to aggregate. We believe that these findings will deepen our understanding of the protein corona.

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