Immobilization of concanavalin A lectin on a reduced graphene oxide-thionine surface by glutaraldehyde crosslinking for the construction of an impedimetric biosensor
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F70883521%3A28110%2F17%3A63516601" target="_blank" >RIV/70883521:28110/17:63516601 - isvavai.cz</a>
Výsledek na webu
<a href="http://www.sciencedirect.com/science/article/pii/S157266571730259X" target="_blank" >http://www.sciencedirect.com/science/article/pii/S157266571730259X</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jelechem.2017.04.019" target="_blank" >10.1016/j.jelechem.2017.04.019</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Immobilization of concanavalin A lectin on a reduced graphene oxide-thionine surface by glutaraldehyde crosslinking for the construction of an impedimetric biosensor
Popis výsledku v původním jazyce
Lectins, which are proteins with selective affinity to glycans or glycoproteins, have been recognized as promising agents for the construction of devices for the detection of specific glycoproteins and for glycoprofiling. This allows for the exploration of new potential biomarkers and for early diagnosis by detection of already known glycosylated biomarkers. In this work, immobilization of Concanavalin A (ConA) lectin on an electrochemically reduced graphene oxide (ErGO)/thionine (Thi) surface via glutaraldehyde (GA) crosslinking is investigated and applied for the impedimetric detection of the glycoprotein invertase (INV). An attachment of ConA/GA aggregates to the ErGO/Thi surface leads to a biosensor with a linear response in the concentration range of 10− 14–10− 8 mol for INV and a sensitivity of 6.1% of RCT change per decade of INV concentration. The sensitivity towards a negative control, i.e., INV with oxidized glycan moieties, is 2.97-fold lower than that towards INV. These findings provide a platform for the development of lectin-based, miniature and cheap biosensors for possible future disease diagnosis.
Název v anglickém jazyce
Immobilization of concanavalin A lectin on a reduced graphene oxide-thionine surface by glutaraldehyde crosslinking for the construction of an impedimetric biosensor
Popis výsledku anglicky
Lectins, which are proteins with selective affinity to glycans or glycoproteins, have been recognized as promising agents for the construction of devices for the detection of specific glycoproteins and for glycoprofiling. This allows for the exploration of new potential biomarkers and for early diagnosis by detection of already known glycosylated biomarkers. In this work, immobilization of Concanavalin A (ConA) lectin on an electrochemically reduced graphene oxide (ErGO)/thionine (Thi) surface via glutaraldehyde (GA) crosslinking is investigated and applied for the impedimetric detection of the glycoprotein invertase (INV). An attachment of ConA/GA aggregates to the ErGO/Thi surface leads to a biosensor with a linear response in the concentration range of 10− 14–10− 8 mol for INV and a sensitivity of 6.1% of RCT change per decade of INV concentration. The sensitivity towards a negative control, i.e., INV with oxidized glycan moieties, is 2.97-fold lower than that towards INV. These findings provide a platform for the development of lectin-based, miniature and cheap biosensors for possible future disease diagnosis.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10406 - Analytical chemistry
Návaznosti výsledku
Projekt
—
Návaznosti
N - Vyzkumna aktivita podporovana z neverejnych zdroju
Ostatní
Rok uplatnění
2017
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Journal of Electroanalytical Chemistry
ISSN
1572-6657
e-ISSN
—
Svazek periodika
794
Číslo periodika v rámci svazku
Neuveden
Stát vydavatele periodika
CH - Švýcarská konfederace
Počet stran výsledku
8
Strana od-do
156-163
Kód UT WoS článku
000403128200022
EID výsledku v databázi Scopus
2-s2.0-85018524623