Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

We performed mass-per-length (MPL) measurements and electron cryomicroscopy (cryo-EM) with 3D reconstruction on an Aβ(1–42) amyloid fibril morphology formed under physiological pH conditions. The data show that the examined Aβ(1–42) fibril morphology has only one protofilament, although two protofilaments were observed with a previously studied Aβ(1–40) fibril. The latter fibril was resolved at 8 Å resolution showing pairs of β-sheets at the cores of the two protofilaments making up a fibril. Detailed comparison of the Aβ(1–42) and Aβ(1–40) fibril structures reveals that they share an axial twofold symmetry and a similar protofilament structure. Furthermore, the MPL data indicate that the protofilaments of the examined Aβ(1–40) and Aβ(1–42) fibrils have the same number of Aβ molecules per cross-β repeat. Based on this data and the previously studied Aβ(1–40) fibril structure, we describe a model for the arrangement of peptides within the Aβ(1–42) fibril.

Bibliography

Schmidt, M., Sachse, C., Richter, W., Xu, C., Fändrich, M., & Grigorieff, N. (2009). Comparison of Alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures. Proceedings of the National Academy of Sciences, 106(47), 19813–19818.

Dates
Type When
Created 15 years, 10 months ago (Oct. 20, 2009, 9:50 p.m.)
Deposited 3 years, 4 months ago (April 12, 2022, 5:11 p.m.)
Indexed 1 minute ago (Sept. 2, 2025, 12:37 p.m.)
Issued 15 years, 9 months ago (Nov. 24, 2009)
Published 15 years, 9 months ago (Nov. 24, 2009)
Published Online 15 years, 9 months ago (Nov. 24, 2009)
Published Print 15 years, 9 months ago (Nov. 24, 2009)
Funders 0

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