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Does polysaccharide glycogen behave as a promoter of amyloid fibril formation at physiologically relevant concentrations?

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    SYSNO ASEP0539969
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleDoes polysaccharide glycogen behave as a promoter of amyloid fibril formation at physiologically relevant concentrations?
    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, ORCID
    Source TitleSoft Matter - ISSN 1744-683X
    Roč. 17, č. 6 (2021), s. 1628-1641
    Number of pages14 s.
    Languageeng - English
    CountryGB - United Kingdom
    Keywordsglycogen ; amyloid fibrils ; chemical modification of polysacchaide
    Subject RIVCD - Macromolecular Chemistry
    OECD categoryPolymer science
    R&D ProjectsLM2015064 GA MŠk - 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 publishingLimited access
    Institutional supportUMCH-V - RVO:61389013
    UT WOS000620242000016
    EID SCOPUS85101150248
    AnnotationWe investigated the influence of glycogen (GG), phytoglycogen (PG), mannan (MAN) and cinnamoyl-modified GG (GG-CIN) on amyloid fibril formation. We used hen egg-white lysozyme (HEWL) as a model system and amyloid beta peptide (1–42) (Aβ1–42) as an Alzheimer's disease-relevant system. For brief detection of fibrils was used thioflavin T (ThT) fluorescence assay and the results were confirmed by transmission electron microscopy (TEM). We also deal with the interaction of polysaccharides and HEWL with isothermal titration calorimetry (ITC) and dynamic light scattering (DLS). We found that all polysaccharides accelerated the formation of amyloid fibrils from both HEWL and Aβ1–42. At high but physiologically relevant concentrations of GG, amyloid fibril formation was extremely accelerated for HEWL. Therefore, on the basis of the herein presented in vitro data, we hypothesize, that dietary D-glucose intake may influence amyloid fibril formation not only by influencing regulatory pathways, but also by direct glycogen-amyloid precursor protein molecular interaction, as glycogen levels in tissues are highly dependent on D-glucose intake.

    WorkplaceInstitute of Macromolecular Chemistry
    ContactEva Čechová, ; Tel.: 296 809 358
    Year of Publishing2022
    Electronic address!divAbstract
Number of the records: 1