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The association of lipids with amyloid fibrils

Sanderson, John M.

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Abstract

Amyloid formation continues to be a widely studied area because of its association with numerous diseases, such as Alzheimer’s and Parkinson’s diseases. Despite a large body of work on protein aggregation and fibril formation, there are still significant gaps in our understanding of the factors that differentiate toxic amyloid formation in vivo from alternative misfolding pathways. In addition to proteins, amyloid fibrils are often associated in their cellular context with several types of molecule, including carbohydrates, polyanions, and lipids. This review focuses in particular on evidence for the presence of lipids in amyloid fibrils and the routes by which those lipids may become incorporated. Chemical analyses of fibril composition, combined with studies to probe the lipid distribution around fibrils, provide evidence that in some cases, lipids have a strong association with fibrils. In addition, amyloid fibrils formed in the presence of lipids have distinct morphologies and material properties. It is argued that lipids are an integral part of many amyloid deposits in vivo, where their presence has the potential to influence the nucleation, morphology, and mechanical properties of fibrils. The role of lipids in these structures is therefore worthy of further study.

Citation

Sanderson, J. M. (2022). The association of lipids with amyloid fibrils. Journal of Biological Chemistry, 298(8), Article 102108. https://doi.org/10.1016/j.jbc.2022.102108

Journal Article Type Article
Acceptance Date Jun 3, 2022
Online Publication Date Jun 7, 2022
Publication Date 2022-08
Deposit Date Oct 27, 2022
Publicly Available Date Apr 23, 2025
Journal Journal of Biological Chemistry
Print ISSN 0021-9258
Electronic ISSN 1083-351X
Publisher American Society for Biochemistry and Molecular Biology
Peer Reviewed Peer Reviewed
Volume 298
Issue 8
Article Number 102108
DOI https://doi.org/10.1016/j.jbc.2022.102108
Public URL https://durham-repository.worktribe.com/output/1188050

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