Chemically modified glycogens: how they influence formation of amyloid fibrils?
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389013%3A_____%2F21%3A00539965" target="_blank" >RIV/61389013:_____/21:00539965 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/21:10442128
Result on the web
<a href="https://pubs.rsc.org/en/content/articlelanding/2021/SM/D0SM01829E#!divAbstract" target="_blank" >https://pubs.rsc.org/en/content/articlelanding/2021/SM/D0SM01829E#!divAbstract</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1039/D0SM01829E" target="_blank" >10.1039/D0SM01829E</a>
Alternative languages
Result language
angličtina
Original language name
Chemically modified glycogens: how they influence formation of amyloid fibrils?
Original language description
The formation of amyloid fibrils from certain proteins stays behind a number of pathologies, so-called amyloidoses. Glycosaminoglycans are polysaccharides and are known natural constituents of amyloids in vivo. However, little is known about the effect of other naturally abundant polysaccharides, and even less is known about the effect of chemically modified polysaccharides on the formation of amyloid fibrils. In the case of low-molecular weight compounds, aromatic substances are known to often influence amyloid formation significantly. We investigated the influence of glycogen (GG) and several modifications of GG with cinnamoyl groups, benzoyl groups and phenylacetyl groups. As model systems, hen egg-white lysozyme (HEWL) and amyloid beta peptide (1–42) (Aβ1–42), which is an Alzheimer disease-relevant system, were used. The fluorescence of thioflavin-T (ThT) was used for the rapid detection of fibrils, and the fluorescence results were confirmed by transmission electron microscopy (TEM). Other techniques, such as isothermal titration calorimetry (ITC) and dynamic light scattering (DLS), were employed to determine the interactions between HEWL and the modifications. We achieved similar results with both model systems (HEWL and Aβ1–42). We showed that π–π interactions played an important role in the process of amyloid fibril formation because fundamental changes were observed in this process even with a very small number of groups containing an aromatic ring. It was found that almost all GG modifications accelerated the formation of amyloid fibrils in both model systems, HEWL and Aβ1–42, except for GG-Ph1 (1.6 mol% phenylacetyl groups), which had a retarding effect compared to all other modifications.n
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
10404 - Polymer science
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
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
Soft Matter
ISSN
1744-683X
e-ISSN
1744-6848
Volume of the periodical
17
Issue of the periodical within the volume
6
Country of publishing house
GB - UNITED KINGDOM
Number of pages
14
Pages from-to
1614-1627
UT code for WoS article
000620242000015
EID of the result in the Scopus database
2-s2.0-85101142282