Structural characterization of conformational transition of amyloid beta peptide promoted on ganglioside clusters

2016 Fiscal Year Final Research Report

• Project/Area Number: 15K21680
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Biophysics; Functional biochemistry
• Research Institution: Okazaki Research Facilities, National Institutes of Natural Sciences
• Principal Investigator: YAGI Maho 大学共同利用機関法人自然科学研究機構(岡崎共通研究施設), 岡崎統合バイオサイエンスセンター, 助教 (40608999)
• Project Period (FY): 2015-04-01 – 2017-03-31
• Keywords: アミロイドβ / ガングリオシド / 固体NMR / 糖脂質 / アルツハイマー病

Outline of Final Research Achievements

In this study, solid-state nuclear magnetic resonance spectroscopy has elucidated the membrane-induced conformation of amyloid (Aβ), in which the disordered N-terminal segment is followed by the stable C-terminal β strand. The data obtained in this project provides insights into the molecular processes of the conformational transition of Aβ coupled with its assembly into parallel β structures.
Structural and kinetic analyses of the Flemish-type mutant (A21G) of Aβ(1-40) peptide were also performed in comparison with the wild type to examine the possible effects of the A21G mutation on the conformation of the Aβ(1-40) isoform. These findings suggest that the mutational perturbation to the membrane binding properties is coupled with the changes in nucleation behavior of Aβ during its fibril formation.

Free Research Field

生物物理学