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How fullerenes inhibit the amyloid fibril formation of hen lysozyme
One-Sun Lee,Viktor I. Petrenko,Katarína Šipošová,Andrey Musatov,Heesoo Park,Senentxu Lanceros-Méndez 한국공업화학회 2022 Journal of Industrial and Engineering Chemistry Vol.106 No.-
The inhibition of protein unfolding and self-assembly into fibrils using nanoparticles is a potential medicinalstrategy to impede amyloid-related diseases. Among various nanoparticles, fullerenes have attractedgreat interest because of their inhibition effect on protein fibrillization, but the mechanism of the inhibitionprocess is not properly understood. To explore the inhibition mechanisms, molecular dynamics simulationsof hen egg white lysozyme (HEWL), a model of an amyloid-prone protein, have been performedin the presence of varied C60 concentrations. It is found that the structural fluctuation of HEWL decreasesas the concentration of C60 increases. As the concentration of C60 increases, clustered fullerene aggregatesare formed via hydrophobic interaction rather than interacting with HEWL, and HEWL was adsorbed onthe surface of the fullerene aggregates. The maintenance of the structure and the inhibition of HEWL fibrillizationby C60 is also experimentally confirmed by thioflavin T fluorescence assays and atomic forcemicroscopy. Thus, two independent methods confirmed that C60 is able to inhibit the formation of amyloidfibrils in a dose-dependent manner. This study is an initial step in understanding by which mechanismC60 inhibits HEWL fibrillization, allowing to further design strategies for amyloid inhibition basedon fullerenes and other nanoparticles.
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