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Does polysaccharide glycogen behave as a promoter of amyloid fibril formation at physiologically relevant concentrations?
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SYSNO ASEP 0539969 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Does 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, ORCIDSource Title Soft Matter - ISSN 1744-683X
Roč. 17, č. 6 (2021), s. 1628-1641Number of pages 14 s. Language eng - English Country GB - United Kingdom Keywords glycogen ; amyloid fibrils ; chemical modification of polysacchaide Subject RIV CD - Macromolecular Chemistry OECD category Polymer science R&D Projects LM2015064 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 publishing Limited access Institutional support UMCH-V - RVO:61389013 UT WOS 000620242000016 EID SCOPUS 85101150248 DOI 10.1039/D0SM01884H Annotation We 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.
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/D0SM01884H#!divAbstract
Number of the records: 1