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Polymorphism of fibrillar structures depending on the size of assembled A beta(17-42) peptides

Title
Polymorphism of fibrillar structures depending on the size of assembled A beta(17-42) peptides
Authors
Cheon, M[Cheon, Mookyung]Kang, M[Kang, Mooseok]Chang, I[Chang, Iksoo]
DGIST Authors
Cheon, M[Cheon, Mookyung]; Kang, M[Kang, Mooseok]; Chang, I[Chang, Iksoo]
Issue Date
2016-11-30
Citation
Scientific Reports, 6
Type
Article
Article Type
Article
ISSN
2045-2322
Abstract
The size of assembled Aβ17-42 peptides can determine polymorphism during oligomerization and fibrillization, but the mechanism of this effect is unknown. Starting from separate random monomers, various fibrillar oligomers with distinct structural characteristics were identified using discontinuous molecular dynamics simulations based on a coarse-grained protein model. From the structures observed in the simulations, two characteristic oligomer sizes emerged, trimer and paranuclei, which generated distinct structural patterns during fibrillization. A majority of the simulations for trimers and tetramers formed non-fibrillar oligomers, which primarily progress to off-pathway oligomers. Pentamers and hexamers were significantly converted into U-shape fibrillar structures, meaning that these oligomers, called paranuclei, might be potent on-pathway intermediates in fibril formation. Fibrillar oligomers larger than hexamers generated substantial polymorphism in which hybrid structures were readily formed and homogeneous fibrillar structures appeared infrequently. © 2016 The Author(s).
URI
http://hdl.handle.net/20.500.11750/2125
DOI
10.1038/srep38196
Publisher
Nature Publishing Group
Related Researcher
  • Author Chang, Ik Soo Theoretical and Computational Biophysics Laboratory
  • Research Interests
Files:
There are no files associated with this item.
Collection:
New BiologyETC1. Journal Articles
Brain and Cognitive SciencesETC1. Journal Articles


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