Alpha-Synuclein Amyloid Aggregation Is Inhibited by Sulfated Aromatic Polymers and Pyridinium Polycation
The effect of a range of synthetic charged polymers on alpha-synuclein aggregation and amyloid formation was tested. Sulfated aromatic polymers, poly(styrene sulfonate) and poly(anethole sulfonate), have been found to suppress the fibril formation. In this case, small soluble complexes, which do not...
Main Authors: | , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2020-02-01
|
Series: | Polymers |
Subjects: | |
Online Access: | https://www.mdpi.com/2073-4360/12/3/517 |
id |
doaj-06925970c6184d15aecf0a4eaac7384c |
---|---|
record_format |
Article |
spelling |
doaj-06925970c6184d15aecf0a4eaac7384c2020-11-25T02:16:10ZengMDPI AGPolymers2073-43602020-02-0112351710.3390/polym12030517polym12030517Alpha-Synuclein Amyloid Aggregation Is Inhibited by Sulfated Aromatic Polymers and Pyridinium PolycationPavel Semenyuk0Lidia Kurochkina1Kseniya Barinova2Vladimir Muronetz3Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, RussiaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, RussiaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, RussiaBelozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119234 Moscow, RussiaThe effect of a range of synthetic charged polymers on alpha-synuclein aggregation and amyloid formation was tested. Sulfated aromatic polymers, poly(styrene sulfonate) and poly(anethole sulfonate), have been found to suppress the fibril formation. In this case, small soluble complexes, which do not bind with thioflavin T, have been formed in contrast to the large stick-type fibrils of free alpha-synuclein. Sulfated polysaccharide (dextran sulfate), as well as sulfated vinylic polymer (poly(vinyl sulfate)) and polycarboxylate (poly(methacrylic acid)), enhanced amyloid aggregation. Conversely, pyridinium polycation, poly(N-ethylvinylpyridinium), switched the mechanism of alpha-synuclein aggregation from amyloidogenic to amorphous, which resulted in the formation of large amorphous aggregates that do not bind with thioflavin T. The obtained results are relevant as a model of charged macromolecules influence on amyloidosis development in humans. In addition, these results may be helpful in searching for new approaches for synucleinopathies treatment with the use of natural polymers.https://www.mdpi.com/2073-4360/12/3/517polyelectrolytesulfated polymersalpha-synucleinamyloid aggregationprotein aggregationartificial chaperone |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Pavel Semenyuk Lidia Kurochkina Kseniya Barinova Vladimir Muronetz |
spellingShingle |
Pavel Semenyuk Lidia Kurochkina Kseniya Barinova Vladimir Muronetz Alpha-Synuclein Amyloid Aggregation Is Inhibited by Sulfated Aromatic Polymers and Pyridinium Polycation Polymers polyelectrolyte sulfated polymers alpha-synuclein amyloid aggregation protein aggregation artificial chaperone |
author_facet |
Pavel Semenyuk Lidia Kurochkina Kseniya Barinova Vladimir Muronetz |
author_sort |
Pavel Semenyuk |
title |
Alpha-Synuclein Amyloid Aggregation Is Inhibited by Sulfated Aromatic Polymers and Pyridinium Polycation |
title_short |
Alpha-Synuclein Amyloid Aggregation Is Inhibited by Sulfated Aromatic Polymers and Pyridinium Polycation |
title_full |
Alpha-Synuclein Amyloid Aggregation Is Inhibited by Sulfated Aromatic Polymers and Pyridinium Polycation |
title_fullStr |
Alpha-Synuclein Amyloid Aggregation Is Inhibited by Sulfated Aromatic Polymers and Pyridinium Polycation |
title_full_unstemmed |
Alpha-Synuclein Amyloid Aggregation Is Inhibited by Sulfated Aromatic Polymers and Pyridinium Polycation |
title_sort |
alpha-synuclein amyloid aggregation is inhibited by sulfated aromatic polymers and pyridinium polycation |
publisher |
MDPI AG |
series |
Polymers |
issn |
2073-4360 |
publishDate |
2020-02-01 |
description |
The effect of a range of synthetic charged polymers on alpha-synuclein aggregation and amyloid formation was tested. Sulfated aromatic polymers, poly(styrene sulfonate) and poly(anethole sulfonate), have been found to suppress the fibril formation. In this case, small soluble complexes, which do not bind with thioflavin T, have been formed in contrast to the large stick-type fibrils of free alpha-synuclein. Sulfated polysaccharide (dextran sulfate), as well as sulfated vinylic polymer (poly(vinyl sulfate)) and polycarboxylate (poly(methacrylic acid)), enhanced amyloid aggregation. Conversely, pyridinium polycation, poly(N-ethylvinylpyridinium), switched the mechanism of alpha-synuclein aggregation from amyloidogenic to amorphous, which resulted in the formation of large amorphous aggregates that do not bind with thioflavin T. The obtained results are relevant as a model of charged macromolecules influence on amyloidosis development in humans. In addition, these results may be helpful in searching for new approaches for synucleinopathies treatment with the use of natural polymers. |
topic |
polyelectrolyte sulfated polymers alpha-synuclein amyloid aggregation protein aggregation artificial chaperone |
url |
https://www.mdpi.com/2073-4360/12/3/517 |
work_keys_str_mv |
AT pavelsemenyuk alphasynucleinamyloidaggregationisinhibitedbysulfatedaromaticpolymersandpyridiniumpolycation AT lidiakurochkina alphasynucleinamyloidaggregationisinhibitedbysulfatedaromaticpolymersandpyridiniumpolycation AT kseniyabarinova alphasynucleinamyloidaggregationisinhibitedbysulfatedaromaticpolymersandpyridiniumpolycation AT vladimirmuronetz alphasynucleinamyloidaggregationisinhibitedbysulfatedaromaticpolymersandpyridiniumpolycation |
_version_ |
1724892275814694912 |