Abundant fish protein inhibits α-synuclein amyloid formation
Artikel i vetenskaplig tidskrift, 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.

Författare

Tony Werner

Chalmers, Biologi och bioteknik, Kemisk biologi

Ranjeet Kumar

Chalmers, Biologi och bioteknik, Kemisk biologi

Istvan Horvath

Chalmers, Biologi och bioteknik, Kemisk biologi

Nathalie Scheers

Chalmers, Biologi och bioteknik, Livsmedelsvetenskap

Pernilla Wittung Stafshede

Chalmers, Biologi och bioteknik, Kemisk biologi

Scientific Reports

2045-2322 (ISSN)

Vol. 8 5465

Ämneskategorier

Strukturbiologi

Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

Läkemedelskemi

DOI

10.1038/s41598-018-23850-0