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Dopamine-Induced Oligomers of α-Synuclein Inhibit Amyloid Fibril Growth and Show No Toxicity

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00572218" target="_blank" >RIV/61388963:_____/23:00572218 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1021/acschemneuro.2c00815" target="_blank" >https://doi.org/10.1021/acschemneuro.2c00815</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acschemneuro.2c00815" target="_blank" >10.1021/acschemneuro.2c00815</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Dopamine-Induced Oligomers of α-Synuclein Inhibit Amyloid Fibril Growth and Show No Toxicity

  • Original language description

    Parkinson’s disease is characterized by the selective death of dopaminergic neurons in the midbrain and accumulation of amyloid fibrils composed of α-synuclein (αSyn). Current treatment involves approaches that compensate the death of dopaminergic neurons by increasing the dopamine levels in remaining cells. However, dopamine can interact with αSyn and produce oligomeric species which were reported to be toxic in many models. We studied formation of dopamine-induced αSyn oligomers and their effect on the αSyn aggregation. Using the Thioflavin T kinetic assay, we have shown that small oligomers efficiently inhibit αSyn fibrillization by binding to fibril ends and blocking the elongation. Moreover, all the fractions of oligomer species proved to be nontoxic in the differentiated SH-SY5Y cell model and showed negligible neurotoxicity on isolated rat synaptosomes. The observed inhibition is an important insight in understanding of dopamine-enhancing therapy on Parkinson’s disease progression and explains the absence of pathology enhancement.

  • 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

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/GJ18-06255Y" target="_blank" >GJ18-06255Y: New strategy for inhibition of amyloid fibril formation</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2023

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    ACS Chemical Neuroscience

  • ISSN

    1948-7193

  • e-ISSN

    1948-7193

  • Volume of the periodical

    14

  • Issue of the periodical within the volume

    11

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    8

  • Pages from-to

    2027-2034

  • UT code for WoS article

    000986696000001

  • EID of the result in the Scopus database

    2-s2.0-85160815145