Facial symmetry in protein self-assembly.
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.
Mehta
Anil K
AK
Center for the Analysis of Supramolecular Self-assemblies, Department of Chemistry, Emory University, Atlanta, Georgia 30322, USA.
Lu
Kun
K
Childers
W Seth
WS
Liang
Yan
Y
Dublin
Steven N
SN
Dong
Jijun
J
Snyder
James P
JP
Pingali
Sai Venkatesh
SV
Thiyagarajan
Pappannan
P
Lynn
David G
DG
D000682:Amyloid / Q000737:chemistry*; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D006860:Hydrogen Bonding; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D043942:Nanotubes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013055:Spectrophotometry, Infrared; D013816:Thermodynamics; D014961:X-Ray Diffraction
D000682:Amyloid; D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C417223:amyloid beta-protein (16-22)