Stewart, KL orcid.org/0000-0001-8845-9155 and Radford, SE orcid.org/0000-0002-3079-8039 (2017) Amyloid Plaques Beyond Aβ: A Survey of the Diverse Modulators of Amyloid Aggregation. Biophysical Reviews, 9 (4). pp. 405-419. ISSN 1867-2450
Abstract
Aggregation of the amyloid-β (Aβ) peptide is strongly correlated with Alzheimer’s disease (AD). Recent research has improved our understanding of the kinetics of amyloid fibril assembly and revealed new details regarding different stages in plaque formation. Presently, interest is turning toward studying this process in a holistic context, focusing on cellular components which interact with the Aβ peptide at various junctures during aggregation, from monomer to cross-β amyloid fibrils. However, even in isolation, a multitude of factors including protein purity, pH, salt content, and agitation affect Aβ fibril formation and deposition, often producing complicated and conflicting results. The failure of numerous inhibitors in clinical trials for AD suggests that a detailed examination of the complex interactions that occur during plaque formation, including binding of carbohydrates, lipids, nucleic acids, and metal ions, is important for understanding the diversity of manifestations of the disease. Unraveling how a variety of key macromolecular modulators interact with the Aβ peptide and change its aggregation properties may provide opportunities for developing therapies. Since no protein acts in isolation, the interplay of these diverse molecules may differentiate disease onset, progression, and severity, and thus are worth careful consideration.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © The Author(s) 2017. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
Keywords: | Alzheimer’s disease; Amyloid plaques; A-beta; Protein aggregation |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Structural Molecular Biology (Leeds) |
Funding Information: | Funder Grant number Wellcome Trust 089311/Z/09/Z BBSRC BB/K01451X/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 26 May 2017 14:54 |
Last Modified: | 23 Jun 2023 22:30 |
Status: | Published |
Publisher: | Springer Verlag |
Identification Number: | 10.1007/s12551-017-0271-9 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:116919 |