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Chemically modified glycogens: how they influence formation of amyloid fibrils?
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SYSNO ASEP 0539965 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Chemically modified glycogens: how they influence formation of amyloid fibrils? Author(s) Holubová, Monika (UMCH-V) ORCID, RID
Lobaz, Volodymyr (UMCH-V) RID, ORCID
Loukotová, Lenka (UMCH-V) RID, ORCID
Rabyk, Mariia (UMCH-V) RID, ORCID
Hromádková, Jiřina (UMCH-V) RID
Trhlíková, Olga (UMCH-V) RID, ORCID
Pechrová, Zdislava (UMCH-V)
Groborz, Ondřej (UMCH-V) ORCID, RID
Štěpánek, Petr (UMCH-V) RID, ORCID
Hrubý, Martin (UMCH-V) RID, ORCIDSource Title Soft Matter - ISSN 1744-683X
Roč. 17, č. 6 (2021), s. 1614-1627Number of pages 14 s. Language eng - English Country GB - United Kingdom Keywords amyloid fibrils ; glycogen ; modification of glycogen Subject RIV CD - Macromolecular Chemistry OECD category Polymer science R&D Projects LM2015064 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA19-01602S GA ČR - Czech Science Foundation (CSF) GA18-07983S GA ČR - Czech Science Foundation (CSF) Method of publishing Limited access Institutional support UMCH-V - RVO:61389013 UT WOS 000620242000015 EID SCOPUS 85101142282 DOI 10.1039/D0SM01829E Annotation 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.
Workplace Institute of Macromolecular Chemistry Contact Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358 Year of Publishing 2022 Electronic address https://pubs.rsc.org/en/content/articlelanding/2021/SM/D0SM01829E#!divAbstract
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