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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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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 |
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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 |
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