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  • Title: Facial symmetry in protein self-assembly.
    Author: Mehta AK, Lu K, Childers WS, Liang Y, Dublin SN, Dong J, Snyder JP, Pingali SV, Thiyagarajan P, Lynn DG.
    Journal: J Am Chem Soc; 2008 Jul 30; 130(30):9829-35. PubMed ID: 18593163.
    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 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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