Anterior gradient-3 protein-antibody interaction at charged interfaces. Label-free chronopotentiometric sensing

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F19%3A00502570" target="_blank" >RIV/68081707:_____/19:00502570 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00209805:_____/19:00078126

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.electacta.2018.12.049" target="_blank" >http://dx.doi.org/10.1016/j.electacta.2018.12.049</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.electacta.2018.12.049" target="_blank" >10.1016/j.electacta.2018.12.049</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Anterior gradient-3 protein-antibody interaction at charged interfaces. Label-free chronopotentiometric sensing

Popis výsledku v původním jazyce

We developed a fast, simple, label-free method useful for the study of interactions between an antibody (Ab) and antigen based on chronopotentiometric stripping analysis and the catalytic hydrogen evolution reaction. The specific interaction of the Ab, adsorbed at a mercury electrode, with AGR3 protein induced a significant increase in chronopotentiometric peak H in comparison to both the CPS response of the Ab alone and that after incubation with nonspecifically binding proteins. Qualitatively similar results were obtained with another polyclonal antibody specific for AGR2 protein. The demonstrated results, along with previous findings indicate that the proposed technique shows promise as a new option for studying the dynamics, not only of surface-attached antibody-antigen complexes, but also other protein-protein interactions. (C) 2018 Elsevier Ltd. All rights reserved.

Název v anglickém jazyce

Anterior gradient-3 protein-antibody interaction at charged interfaces. Label-free chronopotentiometric sensing

Popis výsledku anglicky

We developed a fast, simple, label-free method useful for the study of interactions between an antibody (Ab) and antigen based on chronopotentiometric stripping analysis and the catalytic hydrogen evolution reaction. The specific interaction of the Ab, adsorbed at a mercury electrode, with AGR3 protein induced a significant increase in chronopotentiometric peak H in comparison to both the CPS response of the Ab alone and that after incubation with nonspecifically binding proteins. Qualitatively similar results were obtained with another polyclonal antibody specific for AGR2 protein. The demonstrated results, along with previous findings indicate that the proposed technique shows promise as a new option for studying the dynamics, not only of surface-attached antibody-antigen complexes, but also other protein-protein interactions. (C) 2018 Elsevier Ltd. All rights reserved.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

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OECD FORD obor

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

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

Electrochimica acta

ISSN

0013-4686

e-ISSN

—

Svazek periodika

297

Číslo periodika v rámci svazku

FEB 20 2019

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

6

Strana od-do

974-979

Kód UT WoS článku

000455642500107

EID výsledku v databázi Scopus

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