Abstract
Various cytotoxic mechanisms for neurodegenerative disease are induced by specific conformations of Aβ intermediates. The efforts to understand the diverse intermediate forms of amyloid oligomers have been focused on understanding the aggregation mechanism of specific morphologies for Aβ intermediates. However, these are still not easy tasks to be accomplished because the diverse conformations of Aβ intermediates can be altered during the aggregation process, even though the same Aβ monomers are present. Thus, efforts to reveal the conformational change mechanism could be a fundamental process to understand the formation of diverse Aβ intermediate conformations. Here, we evaluate the conformational characteristics of Aβ17–42 fibrillar oligomers in different environments according to the length. We observed that Aβ fibrillar oligomers optimize their inherent hydrogen bonds and configurational entropy to stabilize their structure according to the simulation time and their length increase. In addition, we revealed the role of the expressed vibration mode shape in the fibrillar oligomers′ elongation and deformation processes. Our results suggest that limitations in amyloid oligomer growth and transformations of their morphologies can be regulated and controlled by modifying the vibration features.
Original language | English |
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Pages (from-to) | 1643-1654 |
Number of pages | 12 |
Journal | ChemPhysChem |
Volume | 19 |
Issue number | 13 |
DOIs | |
Publication status | Published - 2018 Jul 5 |
Bibliographical note
Publisher Copyright:© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
Keywords
- Anchored Aβ fibrillar oligomer
- Aβ aggregation
- Configurational entropy
- Manifested vibration mode shape
- Membrane characteristic
ASJC Scopus subject areas
- Atomic and Molecular Physics, and Optics
- Physical and Theoretical Chemistry