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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389013%3A_____%2F21%3A00539969" target="_blank" >RIV/61389013:_____/21:00539969 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/21:10442129

Výsledek na webu

<a href="https://pubs.rsc.org/en/content/articlelanding/2021/SM/D0SM01884H#!divAbstract" target="_blank" >https://pubs.rsc.org/en/content/articlelanding/2021/SM/D0SM01884H#!divAbstract</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/D0SM01884H" target="_blank" >10.1039/D0SM01884H</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.nn

Název v anglickém jazyce

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

Popis výsledku anglicky

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.nn

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10404 - Polymer science

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Soft Matter

ISSN

1744-683X

e-ISSN

1744-6848

Svazek periodika

17

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

14

Strana od-do

1628-1641

Kód UT WoS článku

000620242000016

EID výsledku v databázi Scopus

2-s2.0-85101150248