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- W4232473085 abstract "On the basis of genetic evidence, biochemical data, and animal models, Aβ has been suggested to be responsible for the pathogenesis of AD. Aβ molecules tend to aggregate to form oligomers, protofibrils (PF), and mature fibrils. Although mature fibrils in the final stage have been thought to be the cause of Alzheimer's disease (AD) pathogenesis, recent studies suggest that Aβ intermediates are more deleterious than are extracellular fibril forms. In order to elucidate the relationships among the soluble state such monomeric, early intermediate state such as PF, and final state such as mature fibrils on Aβ1-42 aggregation pathways in vitro, we used high-speed atomic force microscopy (HS-AFM). In preparation for HS-AFM observation, we separated Aβ1–42 peptides into low- and high-molecular-weight populations (LMW and HMW, respectively) by size exclusion chromatography. The LMW population comprised monomeric and low-order oligomeric Aβ1–42. The HMW population contained protofibrils (PF). We found Aβ1–42 fibrils was mainly formed not from PF but from LMW of Aβ1–42. In addition, we also observed dissociation of single PF to LMW in PF incubation. These results supports that PF is off-pathway aggregate in Aβ fibril formation. We discuss new possible mechanism in the assembly model from soluble state such as monomeric Aβ to final state such as mature fibrils." @default.
- W4232473085 created "2022-05-12" @default.
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- W4232473085 date "2018-07-01" @default.
- W4232473085 modified "2023-10-02" @default.
- W4232473085 title "P2‐219: HIGH‐SPEED ATOMIC FORCE MICROSCOPY REVEALS STRUCTURAL DYNAMICS OF AMYLOID β1‐42 AGGREGATES" @default.
- W4232473085 doi "https://doi.org/10.1016/j.jalz.2018.06.907" @default.
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