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  • Title: S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation.
    Author: Toleikis Z, Ziaunys M, Baranauskiene L, Petrauskas V, Jaudzems K, Smirnovas V.
    Journal: Int J Mol Sci; 2021 Jul 26; 22(15):. PubMed ID: 34360737.
    Abstract:
    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.
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