Cargando…

Abundant fish protein inhibits α-synuclein amyloid formation

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 Parkins...

Descripción completa

Detalles Bibliográficos
Autores principales: Werner, Tony, Kumar, Ranjeet, Horvath, Istvan, Scheers, Nathalie, Wittung-Stafshede, Pernilla
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5882657/
https://www.ncbi.nlm.nih.gov/pubmed/29615738
http://dx.doi.org/10.1038/s41598-018-23850-0
_version_ 1783311491371368448
author Werner, Tony
Kumar, Ranjeet
Horvath, Istvan
Scheers, Nathalie
Wittung-Stafshede, Pernilla
author_facet Werner, Tony
Kumar, Ranjeet
Horvath, Istvan
Scheers, Nathalie
Wittung-Stafshede, Pernilla
author_sort Werner, Tony
collection PubMed
description 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.
format Online
Article
Text
id pubmed-5882657
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-58826572018-04-09 Abundant fish protein inhibits α-synuclein amyloid formation Werner, Tony Kumar, Ranjeet Horvath, Istvan Scheers, Nathalie Wittung-Stafshede, Pernilla Sci Rep Article 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. Nature Publishing Group UK 2018-04-03 /pmc/articles/PMC5882657/ /pubmed/29615738 http://dx.doi.org/10.1038/s41598-018-23850-0 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Werner, Tony
Kumar, Ranjeet
Horvath, Istvan
Scheers, Nathalie
Wittung-Stafshede, Pernilla
Abundant fish protein inhibits α-synuclein amyloid formation
title Abundant fish protein inhibits α-synuclein amyloid formation
title_full Abundant fish protein inhibits α-synuclein amyloid formation
title_fullStr Abundant fish protein inhibits α-synuclein amyloid formation
title_full_unstemmed Abundant fish protein inhibits α-synuclein amyloid formation
title_short Abundant fish protein inhibits α-synuclein amyloid formation
title_sort abundant fish protein inhibits α-synuclein amyloid formation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5882657/
https://www.ncbi.nlm.nih.gov/pubmed/29615738
http://dx.doi.org/10.1038/s41598-018-23850-0
work_keys_str_mv AT wernertony abundantfishproteininhibitsasynucleinamyloidformation
AT kumarranjeet abundantfishproteininhibitsasynucleinamyloidformation
AT horvathistvan abundantfishproteininhibitsasynucleinamyloidformation
AT scheersnathalie abundantfishproteininhibitsasynucleinamyloidformation
AT wittungstafshedepernilla abundantfishproteininhibitsasynucleinamyloidformation