Inactivation of seeding activity of amyloid β‐protein aggregates in vitro

The deposition of amyloid beta-protein (Aβ) in the brain is a major pathological feature of Alzheimer's disease (AD). Recent studies have reported that Aβ pathology can be transmitted among individuals through medical procedures in humans, as well as animal models, and the prevention of Aβ pathology transmission is of great importance to public health. To assess the effect of autoclaving (AC) or gamma (γ)-ray irradiation on Aβ pathology transmission, we evaluated the seeding effect of Aβ aggregates using thioflavin T (ThT) assays and high-speed atomic force microscopy (HS-AFM) and investigated the structural changes in the Aβ aggregates after treatment with AC or γ-ray irradiation using ThT assays, circular dichroism (CD) spectroscopy, and electron microscopy (EM). The ThT assays and HS-AFM showed that the seeding effect of Aβ aggregates was inactivated by AC at different temperatures, exposure times, and concentrations of Aβ aggregates during treatment with AC. The results of the ThT fluorescence and CD spectral patterns of the autoclaved Aβ aggregates indicate that AC reduced β-sheet-rich structures in Aβ aggregates. The EM images demonstrated that the length of the autoclaved Aβ aggregates with fibril-like structures was significantly shorter than that of the untreated ones. Gamma-ray irradiation of Aβ aggregates did not lead to significant inactivation of the Aβ seeding effect or cause structural changes in Aβ aggregates. In conclusion, autoclaving Aβ aggregates decreases β-sheet-rich structures and reduces Aβ seeding activity, which could lead to the development of effective methods for preventing the propagation of Aβ pathology among individuals.

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