S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation |
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| Authors: | Zigmantas Toleikis Mantas Ziaunys Lina Baranauskiene Vytautas Petrauskas Kristaps Jaudzems Vytautas Smirnovas |
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| Affiliation: | 1.Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257 Vilnius, Lithuania; (M.Z.); (L.B.); (V.P.); (V.S.);2.Latvian Institute of Organic Synthesis, Aizkraukles 21, LV-1006 Riga, Latvia; |
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| 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 -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 -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 -synuclein, stabilizing a different structure of -synuclein fibrils. |
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| Keywords: | S100A9 synuclein amyloid proteins fibrils FTIR AFM |
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