Format

Send to

Choose Destination
Sci Rep. 2018 Apr 3;8(1):5465. doi: 10.1038/s41598-018-23850-0.

Abundant fish protein inhibits α-synuclein amyloid formation.

Author information

1
Department of Biology and Biological Engineering, Chalmers University of Technology, 412 96, Gothenburg, Sweden.
2
Department of Biology and Biological Engineering, Chalmers University of Technology, 412 96, Gothenburg, Sweden. Pernilla.wittung@chalmers.se.

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.

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center