Influence of Lipid Membranes on α-Synuclein Aggregation
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00541374" target="_blank" >RIV/61388963:_____/21:00541374 - isvavai.cz</a>
Alternative codes found
RIV/60461373:22340/21:43922489
Result on the web
<a href="https://doi.org/10.1021/acschemneuro.0c00819" target="_blank" >https://doi.org/10.1021/acschemneuro.0c00819</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acschemneuro.0c00819" target="_blank" >10.1021/acschemneuro.0c00819</a>
Alternative languages
Result language
angličtina
Original language name
Influence of Lipid Membranes on α-Synuclein Aggregation
Original language description
α-Synuclein is a neuronal protein involved in synaptic vesicle trafficking. During the course of Parkinson's disease, it aggregates, forming amyloid fibrils that accumulate in the midbrain. This pathological fibrillization process is strongly modulated by physiological interactions of α-synuclein with lipid membranes. However, the detailed mechanism of this effect remains unclear. In this work, we used environment-sensitive fluorescent dyes to study the influence of model lipid membranes on the kinetics of α-synuclein fibrillization. We observed that formation of the fibrils from α-synuclein monomers is strongly delayed even by small amounts of lipids. Furthermore, we found that membrane-bound α-synuclein monomers are not involved in fibril elongation. Hence, presence of lipids slows down fibril growth proportionally to the fraction of membrane-bound protein.
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
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
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
12
Issue of the periodical within the volume
5
Country of publishing house
US - UNITED STATES
Number of pages
6
Pages from-to
825-830
UT code for WoS article
000626321800002
EID of the result in the Scopus database
2-s2.0-85101666075