α-Synuclein Aggregation Is Triggered by Oligomeric Amyloid-β 42 via Heterogeneous Primary Nucleation
OPEN ACCESS
Author / Producer
Date
2023-08-09
Publication Type
Journal Article
ETH Bibliography
yes
Citations
Altmetric
OPEN ACCESS
Data
Rights / License
Abstract
An increasing number of cases where amyloids of different proteins are found in the same patient are being reported. This observation complicates diagnosis and clinical intervention. Amyloids of the amyloid-β peptide or the protein α-synuclein are traditionally considered hallmarks of Alzheimer’s and Parkinson’s diseases, respectively. However, the co-occurrence of amyloids of these proteins has also been reported in patients diagnosed with either disease. Here, we show that soluble species containing amyloid-β can induce the aggregation of α-synuclein. Fibrils formed under these conditions are solely composed of α-synuclein to which amyloid-β can be found associated but not as part of the core of the fibrils. Importantly, by global kinetic analysis, we found that the aggregation of α-synuclein under these conditions occurs via heterogeneous primary nucleation, triggered by soluble aggregates containing amyloid-β.
Permanent link
Publication status
published
External links
Editor
Book title
Journal / series
Volume
145 (33)
Pages / Article No.
18276 - 18285
Publisher
American Chemical Society
Event
Edition / version
Methods
Software
Geographic location
Date collected
Date created
Subject
Organisational unit
09572 - Arosio, Paolo / Arosio, Paolo
Notes
Funding
101002094 - Biologically Inspired Molecular Adhesives towards Multifunctional Biomaterials and Microreactors (EC)