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J Am Chem Soc. 2008 Jul 30;130(30):9829-35. doi: 10.1021/ja801511n. Epub 2008 Jul 2.

Facial symmetry in protein self-assembly.

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Center for the Analysis of Supramolecular Self-assemblies, Department of Chemistry, Emory University, Atlanta, Georgia 30322, USA.


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 Abeta(16-22) peptide, which includes the central core of the Alzheimer's disease Abeta 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 Abeta(16-22) assemblies, amyloid fibers and nanotubes, and define the minimal repeating unit for each assembly.

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