Microscale structural model of Alzheimer A β ( 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 A β (...

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Bibliographic Details
Published in:Applied physics letters 2009-06, Vol.94 (24), p.243904-243904-3
Main Authors: Paparcone, Raffaella, Buehler, Markus J.
Format: Article
Language:English
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Summary: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 A β ( 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.
ISSN:0003-6951
1077-3118
DOI:10.1063/1.3148641