S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation.
AFM
FTIR
S100A9
amyloid proteins
fibrils
synuclein
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
26 Jul 2021
26 Jul 2021
Historique:
received:
29
06
2021
revised:
18
07
2021
accepted:
19
07
2021
entrez:
7
8
2021
pubmed:
8
8
2021
medline:
9
9
2021
Statut:
epublish
Résumé
The formation of amyloid fibril plaques in the brain creates inflammation and neuron death. This process is observed in neurodegenerative disorders, such as Alzheimer's and Parkinson's diseases. Alpha-synuclein is the main protein found in neuronal inclusions of patients who have suffered from Parkinson's disease. S100A9 is a calcium-binding, pro-inflammation protein, which is also found in such amyloid plaques. To understand the influence of S100A9 on the aggregation of α-synuclein, we analyzed their co-aggregation kinetics and the resulting amyloid fibril structure by Fourier-transform infrared spectroscopy and atomic force microscopy. We found that the presence of S100A9 alters the aggregation kinetics of α-synuclein and stabilizes the formation of a particular amyloid fibril structure. We also show that the solution's ionic strength influences the interplay between S100A9 and α-synuclein, stabilizing a different structure of α-synuclein fibrils.
Identifiants
pubmed: 34360737
pii: ijms22157972
doi: 10.3390/ijms22157972
pmc: PMC8348003
pii:
doi:
Substances chimiques
Amyloid
0
Calgranulin B
0
Protein Aggregates
0
Recombinant Proteins
0
S100A9 protein, human
0
SNCA protein, human
0
alpha-Synuclein
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Lietuvos Mokslo Taryba
ID : S-SEN-20-3
Organisme : Lithuania and State Education Development Agency of Latvia
ID : PostDoc Latvia project no. 1.1.1.2/VIAA/2/18/374
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