Skip to Content

Comparison of Alzheimer Aβ(1-40) and Aβ(1-42) amyloid fibrils reveals similar protofilament structures

TitleComparison of Alzheimer Aβ(1-40) and Aβ(1-42) amyloid fibrils reveals similar protofilament structures
Publication TypeJournal Article
Year of Publication2009
AuthorsSchmidt, M, Sachse C, Richter W, Xu C, Fändrich M, Grigorieff N
Refereed DesignationRefereed
JournalProc Natl Acad Sci U S A
Volume106
Issue47
Pagination19813-8
Date Published2009 Nov 24
Abstract

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

Alternate JournalProc. Natl. Acad. Sci. U.S.A.
PreviewAttachmentSize
Schmidt_PNAS2009.pdf3.65 MB