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• W2912558479 abstract "In the amyloid plaques of Alzheimer’s disease (AD) patients, a large number of N-terminal-truncated amyloid β (Aβ) peptides such as Aβ11–40 have been identified in addition to the full-length Aβ peptides. However, little is known about the roles of the N-terminal-truncated peptides in AD pathological process. Herein, seeding and cross-seeding aggregations of Aβ40 and its N-terminal-truncated Aβ11–40 were investigated in the solution and on the surfaces of chips with immobilized seeds by extensive biophysical and biological analyses. The results showed that Aβ40 and Aβ11–40 aggregates could seed both homologous and heterologous aggregations of the two monomers. However, the capability and characteristics of the seeding (homologous aggregation) and cross-seeding (heterologous aggregation) were significantly different. Aβ40 seeds showed stronger acceleration effects on the aggregations than Aβ11–40 seeds and induced β-sheet-rich fibrous aggregates of similar cytotoxicities for the two monomers. This indicates that Aβ40 and Aβ11–40 had similar aggregation pathways in the seeding and cross-seeding on Aβ40 seeds. By contrast, Aβ11–40 seeds led to different aggregation pathways of Aβ40 and Aβ11–40. Pure Aβ11–40 aggregates had higher toxicity than Aβ40 aggregates, and as seeds, Aβ11–40 seeds induced Aβ40 to form aggregates of higher cytotoxicity. However, homologous Aβ11–40 aggregates induced by Aβ11–40 seeds showed lower cytotoxicity than pure Aβ11–40 aggregates. The results suggest that Aβ11–40 plays an important role in the pathological process of AD." @default.
• W2912558479 created "2019-02-21" @default.
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• W2912558479 date "2019-01-25" @default.
• W2912558479 modified "2023-10-11" @default.
• W2912558479 title "Seeding and Cross-Seeding Aggregations of Aβ₄₀ and Its N-Terminal-Truncated Peptide Aβ_11–40" @default.
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• W2912558479 doi "https://doi.org/10.1021/acs.langmuir.8b03599" @default.
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