The influence of zwitterionic and anionic phospholipids on protein aggregation

The progressive aggregation of misfolded proteins is the underlying molecular cause of numerous pathologies including Parkinson's disease and injection and transthyretin amyloidosis. A growing body of evidence indicates that protein deposits detected in organs and tissues of patients diagnosed...

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Published in:Biophysical chemistry 2024-03, Vol.306, p.107174-107174, Article 107174
Main Authors: Ali, Abid, Dou, Tianyi, Holman, Aidan P, Hung, Andrew, Osborne, Luke, Pickett, Davis, Rodriguez, Axell, Zhaliazka, Kiryl, Kurouski, Dmitry
Format: Article
Language:English
Subjects:
alpha-Synuclein - chemistry
Amyloid - chemistry
Amyloidogenic Proteins
Amyloidosis - metabolism
Humans
Parkinson Disease - metabolism
Phospholipids - metabolism
Protein Aggregates
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Summary:The progressive aggregation of misfolded proteins is the underlying molecular cause of numerous pathologies including Parkinson's disease and injection and transthyretin amyloidosis. A growing body of evidence indicates that protein deposits detected in organs and tissues of patients diagnosed with such pathologies contain fragments of lipid membranes. In vitro experiments also showed that lipid membranes could strongly change the aggregation rate of amyloidogenic proteins, as well as alter the secondary structure and toxicity of oligomers and fibrils formed in their presence. In this review, the effect of large unilamellar vesicles (LUVs) composed of zwitterionic and anionic phospholipids on the aggregation rate of insulin, lysozyme, transthyretin (TTR) and α- synuclein (α-syn) will be discussed. The manuscript will also critically review the most recent findings on the lipid-induced changes in the secondary structure of protein oligomers and fibrils, as well as reveal the extent to which lipids could alter the toxicity of protein aggregates formed in their presence.
ISSN:0301-4622
1873-4200
DOI:10.1016/j.bpc.2024.107174