Facial symmetry in protein self-assembly

Anil K. Mehta, Kun Lu, W. Seth Childers, Yan Liang, Steven N. Dublin, Jijun Dong, James P. Snyder, Sai Venkatesh Pingali, Pappannan Thiyagarajan, David G. Lynn

Research output: Contribution to journalArticlepeer-review

222 Scopus citations

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 languageEnglish
Pages (from-to)9829-9835
Number of pages7
JournalJournal of the American Chemical Society
Volume130
Issue number30
DOIs
StatePublished - Jul 30 2008
Externally publishedYes

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