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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

—

Návaznosti

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

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

New Journal of Chemistry

ISSN

1144-0546

e-ISSN

—

Svazek periodika

43

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

13

Strana od-do

3956-3968

Kód UT WoS článku

000459738600038

EID výsledku v databázi Scopus

2-s2.0-85062209868