Inactivation of seeding activity of amyloid β‐protein aggregates in vitro. Issue 4 (7th January 2022)

• Record Type: Journal Article
• Authors: Nakano, Hiroto; Hamaguchi, Tsuyoshi; Ikeda, Tokuhei; Watanabe‐Nakayama, Takahiro; Ono, Kenjiro; Yamada, Masahito
• Is Part Of: Journal of neurochemistry. Volume 160:Issue 4(2022)
• Page Start: 499
• Page End: 516
• Publication Date: 2022-01-07
• Subjects: Neurochemistry -- Periodicals; 616.8042
• DOI: 10.1111/jnc.15563
• Languages: English
• ISSNs: 0022-3042

Abstract

Abstract : Abstract : Our study demonstrates that autoclaving (AC) decreases beta (β)‐sheet‐rich structures in amyloid β‐protein (Aβ) aggregates, which inactivate Aβ seeding activity in vitro. Conformational changes that reduce β‐sheet‐rich structures would be important for understanding the molecular mechanisms underlying the inactivation of seeding activity of Aβ aggregates. Our in vitro study would contribute to the establishment of the inactivation methods for Aβ aggregates to prevent the propagation of Aβ pathology among individuals.