Constant-current chronopotentiometric stripping detection of bovine serum albumin on silver amalgam particles

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F20%3A00524235" target="_blank" >RIV/68081707:_____/20:00524235 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216305:26620/20:PU140098

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/abs/pii/S1572665720300370" target="_blank" >https://www.sciencedirect.com/science/article/abs/pii/S1572665720300370</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jelechem.2020.113854" target="_blank" >10.1016/j.jelechem.2020.113854</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Constant-current chronopotentiometric stripping detection of bovine serum albumin on silver amalgam particles

Popis výsledku v původním jazyce

Highly sensitive peak H registered by constant-current chronopotentiometric stripping (CPS) analysis relates due to the catalytic hydrogen evolution reaction of proteins adsorbed on mercury-based surfaces including recently introduced silver amalgam particles (AgAPs). Since the peak H allows a structure-sensitive analysis of proteins, including those important in biomedicine and cancer research, it has been systematically studied by CPS analysis using AgAPs in this work. Conditions of AgAPs' electrodeposition on basal plane pyrolytic graphite electrode (bPGE) were optimized towards CPS analysis of model protein (bovine serum albumin, BSA) using peak H. Optimized condition for bPGE-AgAP preparation allowed sensitive CPS detection of either native or denatured BSA down to 10 nM concentration, a discrimination between both forms, and registration of the BSA thermal denaturation kinetic. Obtained results have confirmed the applicability of AgAPs in protein electroanalysis and may contribute to the further development of novel (bio)sensors or (bio)electrochemical applications using micro-volume batch, flow-through or lab-on-chip detection systems. (C) 2020 Elsevier B.V. All rights reserved.

Název v anglickém jazyce

Constant-current chronopotentiometric stripping detection of bovine serum albumin on silver amalgam particles

Popis výsledku anglicky

Highly sensitive peak H registered by constant-current chronopotentiometric stripping (CPS) analysis relates due to the catalytic hydrogen evolution reaction of proteins adsorbed on mercury-based surfaces including recently introduced silver amalgam particles (AgAPs). Since the peak H allows a structure-sensitive analysis of proteins, including those important in biomedicine and cancer research, it has been systematically studied by CPS analysis using AgAPs in this work. Conditions of AgAPs' electrodeposition on basal plane pyrolytic graphite electrode (bPGE) were optimized towards CPS analysis of model protein (bovine serum albumin, BSA) using peak H. Optimized condition for bPGE-AgAP preparation allowed sensitive CPS detection of either native or denatured BSA down to 10 nM concentration, a discrimination between both forms, and registration of the BSA thermal denaturation kinetic. Obtained results have confirmed the applicability of AgAPs in protein electroanalysis and may contribute to the further development of novel (bio)sensors or (bio)electrochemical applications using micro-volume batch, flow-through or lab-on-chip detection systems. (C) 2020 Elsevier B.V. All rights reserved.

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

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

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

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

—

Svazek periodika

859

Číslo periodika v rámci svazku

FEB 15 2020

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

5

Strana od-do

113854

Kód UT WoS článku

000521509300011

EID výsledku v databázi Scopus

2-s2.0-85078030466