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  • 标题:Comparison of Alzheimer Aβ(1–40) and Aβ(1–42) amyloid fibrils reveals similar protofilament structures
  • 本地全文:下载
  • 作者:Matthias Schmidt ; Carsten Sachse ; Walter Richter
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2009
  • 卷号:106
  • 期号:47
  • 页码:19813-19818
  • DOI:10.1073/pnas.0905007106
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:We performed mass-per-length (MPL) measurements and electron cryomicroscopy (cryo-EM) with 3D reconstruction on an A{beta}(1-42) amyloid fibril morphology formed under physiological pH conditions. The data show that the examined A{beta}(1-42) fibril morphology has only one protofilament, although two protofilaments were observed with a previously studied A{beta}(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 A{beta}(1-42) and A{beta}(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 A{beta}(1-40) and A{beta}(1-42) fibrils have the same number of A{beta} molecules per cross-{beta} repeat. Based on this data and the previously studied A{beta}(1-40) fibril structure, we describe a model for the arrangement of peptides within the A{beta}(1-42) fibril.
  • 关键词:Alzheimer's disease ; electron microscopy ; prion ; protein folding
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