Abstract
Amyloids are self-assembled protein architectures implicated in dozens of misfolding diseases. These assemblies appear to emerge through a "selection" of specific conformational "strains" which nucleate and propagate within cells to cause disease. The short Aβ(16-22) peptide, which includes the central core of the Alzheimer's disease Aβ peptide, generates an amyloid fiber which is morphologically indistinguishable from the full-length peptide fiber, but it can also form other morphologies under distinct conditions. Here we combine spectroscopic and microscopy analyses that reveal the subtle atomic-level differences that dictate assembly of two conformationally pure Aβ(16-22) assemblies, amyloid fibers and nanotubes, and define the minimal repeating unit for each assembly.
Original language | English |
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Pages (from-to) | 9829-9835 |
Number of pages | 7 |
Journal | Journal of the American Chemical Society |
Volume | 130 |
Issue number | 30 |
DOIs | |
State | Published - Jul 30 2008 |
Externally published | Yes |