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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doaj-c33515d9be4a441cac8d84c97bd065962021-08-06T15:24:56ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-07-01227972797210.3390/ijms22157972S100A9 Alters the Pathway of Alpha-Synuclein Amyloid AggregationZigmantas Toleikis0Mantas Ziaunys1Lina Baranauskiene2Vytautas Petrauskas3Kristaps Jaudzems4Vytautas Smirnovas5Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257 Vilnius, LithuaniaDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257 Vilnius, LithuaniaDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257 Vilnius, LithuaniaDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257 Vilnius, LithuaniaLatvian Institute of Organic Synthesis, Aizkraukles 21, LV-1006 Riga, LatviaDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257 Vilnius, LithuaniaThe 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 <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mi>α</mi></semantics></math></inline-formula>-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 <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mi>α</mi></semantics></math></inline-formula>-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 <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mi>α</mi></semantics></math></inline-formula>-synuclein, stabilizing a different structure of <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mi>α</mi></semantics></math></inline-formula>-synuclein fibrils.https://www.mdpi.com/1422-0067/22/15/7972S100A9synucleinamyloid proteinsfibrilsFTIRAFM |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Zigmantas Toleikis Mantas Ziaunys Lina Baranauskiene Vytautas Petrauskas Kristaps Jaudzems Vytautas Smirnovas |
spellingShingle |
Zigmantas Toleikis Mantas Ziaunys Lina Baranauskiene Vytautas Petrauskas Kristaps Jaudzems Vytautas Smirnovas S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation International Journal of Molecular Sciences S100A9 synuclein amyloid proteins fibrils FTIR AFM |
author_facet |
Zigmantas Toleikis Mantas Ziaunys Lina Baranauskiene Vytautas Petrauskas Kristaps Jaudzems Vytautas Smirnovas |
author_sort |
Zigmantas Toleikis |
title |
S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation |
title_short |
S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation |
title_full |
S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation |
title_fullStr |
S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation |
title_full_unstemmed |
S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation |
title_sort |
s100a9 alters the pathway of alpha-synuclein amyloid aggregation |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2021-07-01 |
description |
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 <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mi>α</mi></semantics></math></inline-formula>-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 <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mi>α</mi></semantics></math></inline-formula>-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 <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mi>α</mi></semantics></math></inline-formula>-synuclein, stabilizing a different structure of <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mi>α</mi></semantics></math></inline-formula>-synuclein fibrils. |
topic |
S100A9 synuclein amyloid proteins fibrils FTIR AFM |
url |
https://www.mdpi.com/1422-0067/22/15/7972 |
work_keys_str_mv |
AT zigmantastoleikis s100a9altersthepathwayofalphasynucleinamyloidaggregation AT mantasziaunys s100a9altersthepathwayofalphasynucleinamyloidaggregation AT linabaranauskiene s100a9altersthepathwayofalphasynucleinamyloidaggregation AT vytautaspetrauskas s100a9altersthepathwayofalphasynucleinamyloidaggregation AT kristapsjaudzems s100a9altersthepathwayofalphasynucleinamyloidaggregation AT vytautassmirnovas s100a9altersthepathwayofalphasynucleinamyloidaggregation |
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1721218313402449920 |