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Big dynorphin is a neuroprotector scaffold against amyloid β-peptide aggregation and cell toxicity
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2022 (English)In: Computational and Structural Biotechnology Journal, E-ISSN 2001-0370, Vol. 20, p. 5672-5679Article in journal (Refereed) Published
Abstract [en]

Amyloid β-peptide (Aβ) misfolding into β-sheet structures triggers neurotoxicity inducing Alzheimer’s disease (AD). Molecules able to reduce or to impair Aβ aggregation are highly relevant as possible AD treatments since they should protect against Aβ neurotoxicity. We have studied the effects of the interaction of dynorphins, a family of opioid neuropeptides, with Aβ40 the most abundant species of Aβ. Biophysical measurements indicate that Aβ40 interacts with Big Dynorphin (BigDyn), lowering the amount of hydrophobic aggregates, and slowing down the aggregation kinetics. As expected, we found that BigDyn protects against Aβ40 aggregates when studied in human neuroblastoma cells by cell survival assays. The cross-interaction between BigDyn and Aβ40 provides insight into the mechanism of amyloid pathophysiology and may open up new therapy possibilities.

Place, publisher, year, edition, pages
2022. Vol. 20, p. 5672-5679
Keywords [en]
Alzheimer’s disease, Amyloid b-peptide, Dynorphins, Peptide therapy, Biophysics
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-212495DOI: 10.1016/j.csbj.2022.10.014ISI: 000930753500004Scopus ID: 2-s2.0-85140094234OAI: oai:DiVA.org:su-212495DiVA, id: diva2:1717085
Available from: 2022-12-07 Created: 2022-12-07 Last updated: 2024-05-31Bibliographically approved

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Król, SylwiaSuades, AlbertGräslund, Astrid

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