Electrochemical sensing of concanavalin A and ovalbumin interaction in solution

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F16%3A00463782" target="_blank" >RIV/68081707:_____/16:00463782 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.aca.2016.06.055" target="_blank" >http://dx.doi.org/10.1016/j.aca.2016.06.055</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.aca.2016.06.055" target="_blank" >10.1016/j.aca.2016.06.055</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Electrochemical sensing of concanavalin A and ovalbumin interaction in solution

Popis výsledku v původním jazyce

In an attempt to develop a label- and reagent-free electrochemical method for the detection of lectin-glycoprotein interactions, we tested lectin-concanavalin A (ConA), glycoprotein-ovalbumin (Ova) and their complex using chronopotentiometric stripping (CPS) analysis and a hanging mercury drop electrode. Incubation of ConA with Ova resulted in an increase of the CPS peak H of the complex as compared to the CPS peaks of individual Ova and ConA proteins. Qualitatively similar results were obtained with other glycoprotein-lectin couples (ConA-RNase B and lectin from Sambucus nigra-fetuin). Using the CPS method, we were able to follow the course of complex formation in solution. Comparable responses of Ova, ConA and ConA-Ova complex were obtained not only at the mercury electrode but also with solid amalgam electrodes, which are more suitable for parallel analysis. It can be anticipated that electrochemical methods, namely CPS, will find application in glycomics and proteomics. (C) 2016 Elsevier B.V. All rights reserved.

Název v anglickém jazyce

Electrochemical sensing of concanavalin A and ovalbumin interaction in solution

Popis výsledku anglicky

In an attempt to develop a label- and reagent-free electrochemical method for the detection of lectin-glycoprotein interactions, we tested lectin-concanavalin A (ConA), glycoprotein-ovalbumin (Ova) and their complex using chronopotentiometric stripping (CPS) analysis and a hanging mercury drop electrode. Incubation of ConA with Ova resulted in an increase of the CPS peak H of the complex as compared to the CPS peaks of individual Ova and ConA proteins. Qualitatively similar results were obtained with other glycoprotein-lectin couples (ConA-RNase B and lectin from Sambucus nigra-fetuin). Using the CPS method, we were able to follow the course of complex formation in solution. Comparable responses of Ova, ConA and ConA-Ova complex were obtained not only at the mercury electrode but also with solid amalgam electrodes, which are more suitable for parallel analysis. It can be anticipated that electrochemical methods, namely CPS, will find application in glycomics and proteomics. (C) 2016 Elsevier B.V. All rights reserved.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

<a href="/cs/project/GA13-00956S" target="_blank" >GA13-00956S: Úloha proteinů rodiny Anterior gradient při vzniku a vývoji nádorových onemocnění</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2016

Kód důvěrnosti údajů

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

Název periodika

Analytica Chimica Acta

ISSN

0003-2670

e-ISSN

—

Svazek periodika

935

Číslo periodika v rámci svazku

SEP2016

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

97-103

Kód UT WoS článku

000382249600007

EID výsledku v databázi Scopus

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