Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
10 11 2020
Historique:
pubmed: 24 10 2020
medline: 8 1 2021
entrez: 23 10 2020
Statut: ppublish

Résumé

Amyloid formation involves the conversion of soluble protein species to an aggregated state. Amyloid fibrils of β-parvalbumin, a protein abundant in fish, act as an allergen but also inhibit the in vitro assembly of the Parkinson protein α-synuclein. However, the intrinsic aggregation mechanism of β-parvalbumin has not yet been elucidated. We performed biophysical experiments in combination with mathematical modeling of aggregation kinetics and discovered that the aggregation of β-parvalbumin is initiated by the formation of dimers stabilized by disulfide bonds and then proceeds via primary nucleation and fibril elongation processes. Dimer formation is accelerated by H

Identifiants

pubmed: 33093204
pii: 2015503117
doi: 10.1073/pnas.2015503117
pmc: PMC7668186
doi:

Substances chimiques

Amyloid 0
Amyloidogenic Proteins 0
Disulfides 0
Parvalbumins 0
Hydrogen Peroxide BBX060AN9V

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

27997-28004

Informations de copyright

Copyright © 2020 the Author(s). Published by PNAS.

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Tony E R Werner (TER)

Department of Biology and Biological Engineering, Chalmers University of Technology, S-41296 Gothenburg, Sweden.

David Bernson (D)

Department of Biology and Biological Engineering, Chalmers University of Technology, S-41296 Gothenburg, Sweden.

Elin K Esbjörner (EK)

Department of Biology and Biological Engineering, Chalmers University of Technology, S-41296 Gothenburg, Sweden.

Sandra Rocha (S)

Department of Biology and Biological Engineering, Chalmers University of Technology, S-41296 Gothenburg, Sweden sandra.rocha@chalmers.se pernilla.wittung@chalmers.se.

Pernilla Wittung-Stafshede (P)

Department of Biology and Biological Engineering, Chalmers University of Technology, S-41296 Gothenburg, Sweden sandra.rocha@chalmers.se pernilla.wittung@chalmers.se.

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Classifications MeSH