| Title |
S100A9 alters the pathway of alpha-synuclein amyloid aggregation / |
| Authors |
Toleikis, Zigmantas ; Žiaunys, Mantas ; Baranauskienė, Lina ; Petrauskas, Vytautas ; Jaudzems, Kristaps ; Smirnovas, Vytautas |
| DOI |
10.3390/ijms22157972 |
| Full Text |
|
| Is Part of |
International journal of molecular sciences.. Basel : MDPI. 2021, vol. 22, no. 15, art. no. 7972, p. [1-13].. eISSN 1422-0067 |
| Keywords [eng] |
AFM ; FTIR ; S100A9 ; amyloid proteins ; fibrils ; synuclein |
| Abstract [eng] |
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. |
| Published |
Basel : MDPI |
| Type |
Journal article |
| Language |
English |
| Publication date |
2021 |
| CC license |
|
