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Big dynorphin is a neuroprotector scaffold against amyloid β-peptide aggregation and cell toxicity

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 th...

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Autores principales: Gallego-Villarejo, Lucía, Wallin, Cecilia, Król, Sylwia, Enrich-Bengoa, Jennifer, Suades, Albert, Aguilella-Arzo, Marcel, Gomara, María José, Haro, Isabel, Wärmlander, Sebastian, Muñoz, Francisco J., Gräslund, Astrid, Perálvarez-Marín, Alex
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9582793/
https://www.ncbi.nlm.nih.gov/pubmed/36284704
http://dx.doi.org/10.1016/j.csbj.2022.10.014
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author Gallego-Villarejo, Lucía
Wallin, Cecilia
Król, Sylwia
Enrich-Bengoa, Jennifer
Suades, Albert
Aguilella-Arzo, Marcel
Gomara, María José
Haro, Isabel
Wärmlander, Sebastian
Muñoz, Francisco J.
Gräslund, Astrid
Perálvarez-Marín, Alex
author_facet Gallego-Villarejo, Lucía
Wallin, Cecilia
Król, Sylwia
Enrich-Bengoa, Jennifer
Suades, Albert
Aguilella-Arzo, Marcel
Gomara, María José
Haro, Isabel
Wärmlander, Sebastian
Muñoz, Francisco J.
Gräslund, Astrid
Perálvarez-Marín, Alex
author_sort Gallego-Villarejo, Lucía
collection PubMed
description 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 Aβ(40) the most abundant species of Aβ. Biophysical measurements indicate that Aβ(40) 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 Aβ(40) aggregates when studied in human neuroblastoma cells by cell survival assays. The cross-interaction between BigDyn and Aβ(40) provides insight into the mechanism of amyloid pathophysiology and may open up new therapy possibilities.
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spelling pubmed-95827932022-10-24 Big dynorphin is a neuroprotector scaffold against amyloid β-peptide aggregation and cell toxicity Gallego-Villarejo, Lucía Wallin, Cecilia Król, Sylwia Enrich-Bengoa, Jennifer Suades, Albert Aguilella-Arzo, Marcel Gomara, María José Haro, Isabel Wärmlander, Sebastian Muñoz, Francisco J. Gräslund, Astrid Perálvarez-Marín, Alex Comput Struct Biotechnol J Special Issue articles from "Peptide structural conversions and cross-interactions in health and disease" edited by Alex Perálvarez-Marín 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 Aβ(40) the most abundant species of Aβ. Biophysical measurements indicate that Aβ(40) 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 Aβ(40) aggregates when studied in human neuroblastoma cells by cell survival assays. The cross-interaction between BigDyn and Aβ(40) provides insight into the mechanism of amyloid pathophysiology and may open up new therapy possibilities. Research Network of Computational and Structural Biotechnology 2022-10-14 /pmc/articles/PMC9582793/ /pubmed/36284704 http://dx.doi.org/10.1016/j.csbj.2022.10.014 Text en © 2022 The Authors. Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology. https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Special Issue articles from "Peptide structural conversions and cross-interactions in health and disease" edited by Alex Perálvarez-Marín
Gallego-Villarejo, Lucía
Wallin, Cecilia
Król, Sylwia
Enrich-Bengoa, Jennifer
Suades, Albert
Aguilella-Arzo, Marcel
Gomara, María José
Haro, Isabel
Wärmlander, Sebastian
Muñoz, Francisco J.
Gräslund, Astrid
Perálvarez-Marín, Alex
Big dynorphin is a neuroprotector scaffold against amyloid β-peptide aggregation and cell toxicity
title Big dynorphin is a neuroprotector scaffold against amyloid β-peptide aggregation and cell toxicity
title_full Big dynorphin is a neuroprotector scaffold against amyloid β-peptide aggregation and cell toxicity
title_fullStr Big dynorphin is a neuroprotector scaffold against amyloid β-peptide aggregation and cell toxicity
title_full_unstemmed Big dynorphin is a neuroprotector scaffold against amyloid β-peptide aggregation and cell toxicity
title_short Big dynorphin is a neuroprotector scaffold against amyloid β-peptide aggregation and cell toxicity
title_sort big dynorphin is a neuroprotector scaffold against amyloid β-peptide aggregation and cell toxicity
topic Special Issue articles from "Peptide structural conversions and cross-interactions in health and disease" edited by Alex Perálvarez-Marín
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9582793/
https://www.ncbi.nlm.nih.gov/pubmed/36284704
http://dx.doi.org/10.1016/j.csbj.2022.10.014
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