Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins.
Alzheimer
Neurokinin B
Parkinson
amyloid
copper
diabetes
misfolding
prion
synuclein
tau
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
05 Sep 2023
05 Sep 2023
Historique:
received:
31
07
2023
revised:
30
08
2023
accepted:
03
09
2023
medline:
4
10
2023
pubmed:
28
9
2023
entrez:
28
9
2023
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 37764220
pii: molecules28186446
doi: 10.3390/molecules28186446
pmc: PMC10537474
pii:
doi:
Substances chimiques
Amyloidogenic Proteins
0
Copper
789U1901C5
Protein Aggregates
0
Amyloid beta-Peptides
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
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