Abundant fish protein inhibits α-synuclein amyloid formation.

Werner T, Kumar R, Horvath I, Scheers N, Wittung-Stafshede P

Sci Rep 8 (1) 5465 [2018-04-03; online 2018-04-03]

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.

Integrated Microscopy Technologies Gothenburg [Service]

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PubMed 29615738

DOI 10.1038/s41598-018-23850-0

Crossref 10.1038/s41598-018-23850-0

pii: 10.1038/s41598-018-23850-0
pmc: PMC5882657