Non-uniform self-assembly: On the anisotropic architecture of alpha-synuclein supra-fibrillar aggregates
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00478232" target="_blank" >RIV/61388963:_____/17:00478232 - isvavai.cz</a>
Result on the web
<a href="https://www.nature.com/articles/s41598-017-06532-1" target="_blank" >https://www.nature.com/articles/s41598-017-06532-1</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41598-017-06532-1" target="_blank" >10.1038/s41598-017-06532-1</a>
Alternative languages
Result language
angličtina
Original language name
Non-uniform self-assembly: On the anisotropic architecture of alpha-synuclein supra-fibrillar aggregates
Original language description
Although the function of biopolymer hydrogels in nature depends on structural anisotropy at mesoscopic length scales, the self-assembly of such anisotropic structures in vitro is challenging. Here we show that fibrils of the protein alpha-synuclein spontaneously self-assemble into structurally anisotropic hydrogel particles. While the fibrils in the interior of these supra-fibrillar aggregates (SFAs) are randomly oriented, the fibrils in the periphery prefer to cross neighboring fibrils at high angles. This difference in organization coincides with a significant difference in polarity of the environment in the central and peripheral parts of the SFA. We rationalize the structural anisotropy of SFAs in the light of the observation that alpha S fibrils bind a substantial amount of counterions. We propose that, with the progress of protein polymerization into fibrils, this binding of counterions changes the ionic environment which triggers a change in fibril organization resulting in anisotropy in the architecture of hydrogel particles.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Scientific Reports
ISSN
2045-2322
e-ISSN
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Volume of the periodical
7
Issue of the periodical within the volume
Aug 9
Country of publishing house
GB - UNITED KINGDOM
Number of pages
11
Pages from-to
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UT code for WoS article
000407294200056
EID of the result in the Scopus database
2-s2.0-85027136128