In the latest study of Alzheimer’s disease, the small oligomers formed by Amyloid-β (Aβ) peptide were supposed to be the main toxic species for the neurone. Our lab kept focusing on the structural study of a stable 150-kDa Aβ(1-42) oligomer. Previously, we found two β-strand regions on the Aβ(1-42) sequence, the C-strand (A30 – A42) and the N-strand (E11 – V24), and the C-strands were found to form an antiparallel β-sheet with the center at V36. The most recent solid state NMR constraints indicate the N-strands would assemble into an out-of-register parallel β-sheet, which has uncommon registry shifts of alternating +3 and -3.<br/>At the meantime, the preliminary Cryo-EM class averages of the oligomer sample showed it has 4-fold symmetry. We proposed one reasonable structure based on the symmetry and the two β-sheet configurations, which also matches the dimension of the Cryo-EM data. A dimer-addition mechanism was proposed to explain the stability and the size limitation of the oligomer.

Use solid state nmr to characterize the structure of aβ<sub>1-42 </sub>150-kDa oligomers: Anti-parallel β-sheet and a special parallel β-sheet

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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Use solid state nmr to characterize the structure of aβ1-42 150-kDa oligomers: Anti-parallel β-sheet and a special parallel β-sheet

Use solid state nmr to characterize the structure of aβ_1-42150-kDa oligomers: Anti-parallel β-sheet and a special parallel β-sheet