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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10610 - Biophysics

Result continuities

  • Project

  • 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

  • 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

  • UT code for WoS article

    000407294200056

  • EID of the result in the Scopus database

    2-s2.0-85027136128