Binding and inhibitory effect of the food colorants Sunset Yellow and Ponceau 4R on amyloid fibrillation of lysozyme

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F19%3A00109308" target="_blank" >RIV/00216224:14740/19:00109308 - isvavai.cz</a>

Result on the web

<a href="https://pubs.rsc.org/en/content/articlelanding/2019/NJ/C8NJ05827J#!divAbstract" target="_blank" >https://pubs.rsc.org/en/content/articlelanding/2019/NJ/C8NJ05827J#!divAbstract</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c8nj05827j" target="_blank" >10.1039/c8nj05827j</a>

Result language

angličtina

Original language name

Binding and inhibitory effect of the food colorants Sunset Yellow and Ponceau 4R on amyloid fibrillation of lysozyme

Original language description

Amyloid fibrillogenesis of proteins is known to be the root cause of a large number of diseases like Parkinson's, Alzheimer's, and Huntington's disease, spongiform encephalopathy, amyloid polyneuropathy, type-II diabetes, etc. In the present work, the impact of Sunset Yellow (SY) and Ponceau 4R (P4R) food colorants on amyloid fibrillation of lysozyme (Lyz) under acidic pH and high temperature was studied using Thioflavin T (ThT) fluorescence, Congo Red (CR) assay, circular dichroism (CD) spectroscopy, transmission electron microscopy (TEM) and field emission scanning electron microscopy (FESEM). The results illustrated that SY and P4R inhibited the formation of amyloid fibrils. In addition, the binding between food colorants (SY and P4R) and Lyz was investigated using various spectroscopic methods such as fluorescence, absorption and CD spectroscopy along with theoretical approaches (such as docking and simulation). The binding results suggested that P4R has a remarkably higher binding affinity for Lyz in comparison to SY. In summary, we hope the in vitro fibrillation and interaction studies in the presence of food colorants (SY and P4R) are helpful to gain a better understanding about the mechanism of amyloid fibril formation and interaction at the molecular level.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10406 - Analytical chemistry

Project

—

Continuities

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2019

Confidentiality

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

Name of the periodical

New Journal of Chemistry

ISSN

1144-0546

e-ISSN

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Volume of the periodical

43

Issue of the periodical within the volume

9

Country of publishing house

GB - UNITED KINGDOM

Number of pages

13

Pages from-to

3956-3968

UT code for WoS article

000459738600038

EID of the result in the Scopus database

2-s2.0-85062209868