Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 130, Issue 30, Pages 9829-9835Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja801511n
Keywords
-
Categories
Ask authors/readers for more resources
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 A beta(16-22) peptide, which includes the central core of the Alzheimer's disease A beta 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 A beta(16-22) assemblies, amyloid fibers and nanotubes, and define the minimal repeating unit for each assembly.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available