| 研究実績の概要 |
I extended my study on protein aggregation from globular proteins to an intrinsically disordered protein, amyloid beta 1-40, this year. Misfolding and aggregation of amyloid beta 1-40 has been related to the onset of Alzheimer’s disease. Although much has been done to explore amyloid beta 1-40 aggregation, its detail mechanism is only partially understood.
I investigated the microscopic mechanism and pathway of amyloid beta 1-40 aggregation with macroscopic viewpoints using alcohols with the application of ultrasonication. The results suggested that the microscopic aggregation pathways of amyloid beta 1-40 depended on concentration and type of alcohols. Moreover, the addition of salts induced conversion of amyloid beta 1-40 from off-pathway oligomers into in-pathways protofibrils. Based on experimental results, I constructed phase diagrams of amyloid beta 1-40 aggregation in alcohols, which indicated that the concept of solubility and supersaturation also provided a macroscopic understanding of amyloid beta 1-40 aggregation.
In conclusion, these results gave a further insight into the aggregation process of amyloid beta 1-40, which is beneficial for developing small molecules to control amyloid beta 1-40 aggregation.
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