The nanoparticle protein corona influences the interaction at the bio-nano interface, which ultimately affects the biological responses of the cells to nanoparticles. The composition of protein corona has been extensively studied, and their compositional change over time has also been reported. It has also suggested that protein unfolding at the nanoparticle interface can occur, but no in situ evidences have yet been reported. It is still not known how the protein absorption kinetics is related to the structural changes of the proteins. The structural changes of the adsorbed proteins could lead to adverse physiological effects because it is known that protein unfolding has a direct link to some neurodegenerative diseases. Thus it is imperative to study the dynamics and the heterogeneity of the protein corona at the level of single proteins. By combined analysis using fluorescence correlation spectroscopy, super resolution spectroscopy and CD spectroscopy, we demonstrate the relationship between the residence time and the probability of protein unfolding at the nanoparticle interface. This study also provides insight into competitive binding dynamics and conformational changes of protein in blood plasma.

Probing the dynamic and structure of nanoparticle protein corona by using single molecule spectroscopy

249th National Meeting (2015)

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