Počet záznamů: 1
Chemically modified glycogens: how they influence formation of amyloid fibrils?
- 1.
SYSNO ASEP 0539965 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Chemically modified glycogens: how they influence formation of amyloid fibrils? Tvůrce(i) 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, ORCIDZdroj.dok. Soft Matter - ISSN 1744-683X
Roč. 17, č. 6 (2021), s. 1614-1627Poč.str. 14 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova amyloid fibrils ; glycogen ; modification of glycogen Vědní obor RIV CD - Makromolekulární chemie Obor OECD Polymer science CEP LM2015064 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GA19-01602S GA ČR - Grantová agentura ČR GA18-07983S GA ČR - Grantová agentura ČR Způsob publikování Omezený přístup Institucionální podpora UMCH-V - RVO:61389013 UT WOS 000620242000015 EID SCOPUS 85101142282 DOI 10.1039/D0SM01829E Anotace 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.
Pracoviště Ústav makromolekulární chemie Kontakt Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358 Rok sběru 2022 Elektronická adresa https://pubs.rsc.org/en/content/articlelanding/2021/SM/D0SM01829E#!divAbstract
Počet záznamů: 1