Hypothesis: The process of protein corona changes has been widely believed to follow the Vroman effect, while protein structural change during the process is rarely reported, due to the lack of analytical methods. In-situ interpretation for protein structural change is critical to processes such as the recognition and transport of nanomaterials.
Experiments: Molecular dynamics (MD) simulation was used to predict the deflection and twist of the protein tertiary structure. The structural changes of the surface protein corona during the interaction of nanoparticles (NPs) with lipid bilayer were probed in situ and real-time by sum frequency generation (SFG) spectroscopy.
Findings: The ring tertiary structure of the protein corona is altered from vertical to horizontal on particle surface, a process of the soft-to-hard structural transition, which is contributed by the hydrogen bonding force between the protein and water molecules. The negatively charged protein corona can induce the redistribution of interfacial charge, leading to a more stable hydrogen bond network of the interfacial water. Our findings suggest that the structural change from flexible to rigid is a crucial process in the soft-to-hard transition of the protein corona, which will be a beneficial supplement to the Vroman effect of protein adsorption.
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