Title |
Abundant fish protein inhibits α-synuclein amyloid formation
|
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Published in |
Scientific Reports, April 2018
|
DOI | 10.1038/s41598-018-23850-0 |
Pubmed ID | |
Authors |
Tony Werner, Ranjeet Kumar, Istvan Horvath, Nathalie Scheers, Pernilla Wittung-Stafshede |
Abstract |
The most common allergen in fish, the highly-abundant protein β-parvalbumin, forms amyloid structures as a way to avoid gastrointestinal degradation and transit to the blood. In humans, the same amyloid structures are mostly associated with neurodegenerative disorders such as Alzheimer's and Parkinson's. We here assessed a putative connection between these amyloids using recombinant Atlantic cod β-parvalbumin and the key amyloidogenic protein in Parkinson's disease, α-synuclein. Using a set of in vitro biophysical methods, we discovered that β-parvalbumin readily inhibits amyloid formation of α-synuclein. The underlying mechanism was found to involve α-synuclein binding to the surface of β-parvalbumin amyloid fibers. In addition to being a new amyloid inhibition mechanism, the data suggest that health benefits of fish may be explained in part by cross-reaction of β-parvalbumin with human amyloidogenic proteins. |
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Demographic breakdown
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Science communicators (journalists, bloggers, editors) | 1 | 2% |
Mendeley readers
Geographical breakdown
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Demographic breakdown
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Student > Bachelor | 7 | 14% |
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Other | 5 | 10% |
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