To study the effect of mechanical shocks on the neurodegenerative-related fibril-formation protein, the aggregation process, especially the initial oligomerization of a model yeast prion protein Sup35NM, was followed and analyzed by using a combination of laser light scattering, the Smoluchowski coagulation analysis, Thioflavin T fluorescence assay, and transmission electron microscopy. We find that an initial short-time mechanical shock (ultrasonication or circular shaking) affects the in vitro association kinetics of neurodegenerative-related Sup35NM proteins in dilute PBS solutions by generating a relatively larger number of smaller non-structured oligomers that further serve as tiny "crystallization" seeds in promoting the formation of longer fibrils. Our study provides an effective and quantitative method to investigate the initial oligomerization kinetics of amyloid fibrils formation. Furthermore, the current results may shed light on the molecular understanding on how environmental factors increase the risk of neurodegenerative diseases such as dementia.
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