Microscale structural model of Alzheimer Aβ(1-40) amyloid fibril

Amyloid fibril formation and characterization are crucial due to their association with severe degenerative disorders such as Alzheimer's, type II diabetes, and Parkinson's disease. Here we present an atomistic-based multiscale analysis, utilized to predict the structure of Alzheimer Aβ(1-...

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Bibliographic Details
Main Authors: Paparcone, Raffaella (Contributor), Buehler, Markus J (Author)
Other Authors: Massachusetts Institute of Technology. Department of Civil and Environmental Engineering (Contributor), Massachusetts Institute of Technology. Laboratory for Atomistic and Molecular Mechanics (Contributor), Buehler, Markus J. (Contributor)
Format: Article
Language:English
Published: American Institute of Physics (AIP), 2013-02-28T19:48:56Z.
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Online Access:Get fulltext
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100 1 0 |a Paparcone, Raffaella  |e author 
100 1 0 |a Massachusetts Institute of Technology. Department of Civil and Environmental Engineering  |e contributor 
100 1 0 |a Massachusetts Institute of Technology. Laboratory for Atomistic and Molecular Mechanics  |e contributor 
100 1 0 |a Paparcone, Raffaella  |e contributor 
100 1 0 |a Buehler, Markus J.  |e contributor 
700 1 0 |a Buehler, Markus J  |e author 
245 0 0 |a Microscale structural model of Alzheimer Aβ(1-40) amyloid fibril 
260 |b American Institute of Physics (AIP),   |c 2013-02-28T19:48:56Z. 
856 |z Get fulltext  |u http://hdl.handle.net/1721.1/77244 
520 |a Amyloid fibril formation and characterization are crucial due to their association with severe degenerative disorders such as Alzheimer's, type II diabetes, and Parkinson's disease. Here we present an atomistic-based multiscale analysis, utilized to predict the structure of Alzheimer Aβ(1-40) fibrils. Our study provides a structural model of amyloid fibers with lengths of hundreds of nanometers at atomistic resolution. We report a systematic analysis of the energies, structural changes and H-bonding for varying fibril lengths, elucidating their size dependent properties. Our model predicts the formation of twisted amyloid microfibers with a periodicity of ≈82 nm, in close agreement with experimental results. 
520 |a United States. Office of Naval Research (Grant NN00014-08-1-0844) 
546 |a en_US 
655 7 |a Article 
773 |t Applied Physics Letters