Abundant fish protein inhibits α-synuclein amyloid formation
Journal article, 2018

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.

Author

Tony Werner

Chalmers, Biology and Biological Engineering, Chemical Biology

Ranjeet Kumar

Chalmers, Biology and Biological Engineering, Chemical Biology

Istvan Horvath

Chalmers, Biology and Biological Engineering, Chemical Biology

Nathalie Scheers

Chalmers, Biology and Biological Engineering, Food and Nutrition Science

Pernilla Wittung Stafshede

Chalmers, Biology and Biological Engineering, Chemical Biology

Scientific Reports

2045-2322 (ISSN)

Vol. 8 1 5465

Subject Categories

Structural Biology

Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

Medicinal Chemistry

DOI

10.1038/s41598-018-23850-0

More information

Latest update

4/18/2018