Cargando…

Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins

Amyloid diseases have become a global concern due to their increasing prevalence. Transition metals, including copper, can affect the aggregation of the pathological proteins involved in these diseases. Copper ions play vital roles in organisms, but the disruption of their homeostasis can negatively...

Descripción completa

Detalles Bibliográficos
Autor principal: Oliveri, Valentina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10537474/
https://www.ncbi.nlm.nih.gov/pubmed/37764220
http://dx.doi.org/10.3390/molecules28186446
_version_ 1785113111493083136
author Oliveri, Valentina
author_facet Oliveri, Valentina
author_sort Oliveri, Valentina
collection PubMed
description Amyloid diseases have become a global concern due to their increasing prevalence. Transition metals, including copper, can affect the aggregation of the pathological proteins involved in these diseases. Copper ions play vital roles in organisms, but the disruption of their homeostasis can negatively impact neuronal function and contribute to amyloid diseases with toxic protein aggregates, oxidative stress, mitochondrial dysfunction, impaired cellular signaling, inflammation, and cell death. Gaining insight into the imbalance of copper ions and its impact on protein folding and aggregation is crucial for developing focused therapies. This review examines the influence of copper ions on significant amyloid proteins/peptides, offering a comprehensive overview of the current understanding in this field.
format Online
Article
Text
id pubmed-10537474
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-105374742023-09-29 Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins Oliveri, Valentina Molecules Review Amyloid diseases have become a global concern due to their increasing prevalence. Transition metals, including copper, can affect the aggregation of the pathological proteins involved in these diseases. Copper ions play vital roles in organisms, but the disruption of their homeostasis can negatively impact neuronal function and contribute to amyloid diseases with toxic protein aggregates, oxidative stress, mitochondrial dysfunction, impaired cellular signaling, inflammation, and cell death. Gaining insight into the imbalance of copper ions and its impact on protein folding and aggregation is crucial for developing focused therapies. This review examines the influence of copper ions on significant amyloid proteins/peptides, offering a comprehensive overview of the current understanding in this field. MDPI 2023-09-05 /pmc/articles/PMC10537474/ /pubmed/37764220 http://dx.doi.org/10.3390/molecules28186446 Text en © 2023 by the author. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Oliveri, Valentina
Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins
title Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins
title_full Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins
title_fullStr Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins
title_full_unstemmed Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins
title_short Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins
title_sort unveiling the effects of copper ions in the aggregation of amyloidogenic proteins
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10537474/
https://www.ncbi.nlm.nih.gov/pubmed/37764220
http://dx.doi.org/10.3390/molecules28186446
work_keys_str_mv AT oliverivalentina unveilingtheeffectsofcopperionsintheaggregationofamyloidogenicproteins