Fetuin and asialofetuin at charged surfaces: Influence of sialic acid presence

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F21%3A00549591" target="_blank" >RIV/68081707:_____/21:00549591 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S1572665721008274?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S1572665721008274?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jelechem.2021.115801" target="_blank" >10.1016/j.jelechem.2021.115801</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Fetuin and asialofetuin at charged surfaces: Influence of sialic acid presence

Popis výsledku v původním jazyce

Major human diseases are associated with changes in glycosylation. The sialic acid is highly expressed saccharide residue typically terminating branches of protein glycans and glycosphingolipids. Here we compared sialoprotein fetuin with its desialylated form asialofetuin using label-free constant current chronopotentiometric stripping (CPS) analysis and impedance C-t curves to better understand the behavior of glycoproteins at charged surfaces. Electrochemistry represents useful tool for study of molecules at charged surfaces. Using CPS peak H, we show that the terminal sialic acids presence in glycans of fetuin stabilizes its molecule against effects of electric field. Additionally the presence of negatively charged sialic acid prevents an interaction between glycoprotein and negatively charged electrode. The different behavior of the glycoproteins according to sialic acid content can also be used for easy determination of sialoglycoproteins.

Název v anglickém jazyce

Fetuin and asialofetuin at charged surfaces: Influence of sialic acid presence

Popis výsledku anglicky

Major human diseases are associated with changes in glycosylation. The sialic acid is highly expressed saccharide residue typically terminating branches of protein glycans and glycosphingolipids. Here we compared sialoprotein fetuin with its desialylated form asialofetuin using label-free constant current chronopotentiometric stripping (CPS) analysis and impedance C-t curves to better understand the behavior of glycoproteins at charged surfaces. Electrochemistry represents useful tool for study of molecules at charged surfaces. Using CPS peak H, we show that the terminal sialic acids presence in glycans of fetuin stabilizes its molecule against effects of electric field. Additionally the presence of negatively charged sialic acid prevents an interaction between glycoprotein and negatively charged electrode. The different behavior of the glycoproteins according to sialic acid content can also be used for easy determination of sialoglycoproteins.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)

Projekt

<a href="/cs/project/GA18-18154S" target="_blank" >GA18-18154S: Nové nástroje elektrochemické analýzy proteinových interakcí s nukleovými kyselinami a proteiny nevyžadující značení</a><br>

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

Journal of Electroanalytical Chemistry

ISSN

1572-6657

e-ISSN

1873-2569

Svazek periodika

902

Číslo periodika v rámci svazku

DEC 1 2021

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

7

Strana od-do

115801

Kód UT WoS článku

000718944400014

EID výsledku v databázi Scopus

2-s2.0-85118335371