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Abundant fish protein inhibits ?-synuclein amyloid formation.

ABSTRACT: The most common allergen in fish, the highly-abundant protein ?-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 ?-parvalbumin and the key amyloidogenic protein in Parkinson's disease, ?-synuclein. Using a set of in vitro biophysical methods, we discovered that ?-parvalbumin readily inhibits amyloid formation of ?-synuclein. The underlying mechanism was found to involve ?-synuclein binding to the surface of ?-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 ?-parvalbumin with human amyloidogenic proteins.

SUBMITTER: Werner T

PROVIDER: S-EPMC5882657 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature

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Abundant fish protein inhibits α-synuclein amyloid formation.

Werner Tony T Kumar Ranjeet R Horvath Istvan I Scheers Nathalie N Wittung-Stafshede Pernilla P

Scientific reports 20180403 1

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 i ...[more]

PMID: 29615738

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