S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation

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 Parki...

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Bibliographic Details
Published in:International journal of molecular sciences 2021-08, Vol.22 (15), p.7972
Main Authors: Toleikis, Zigmantas, Ziaunys, Mantas, Baranauskiene, Lina, Petrauskas, Vytautas, Jaudzems, Kristaps, Smirnovas, Vytautas
Format: Article
Language:English
Subjects:
AFM
Alzheimer's disease
amyloid proteins
Atomic force microscopy
Calcium
Cell death
Fibrils
FTIR
Hydrogen
Inclusions
Infrared spectroscopy
Ionic strength
Kinetics
Parkinson's disease
Physiology
Plaques
Population
Proteins
S100A9
Spectrum analysis
Synuclein
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Summary: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.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms22157972