Modification of a Mercury Electrode with Different Thioalkanes: Structure-Sensitive Bovine Serum Albumin Analysis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F18%3A00491232" target="_blank" >RIV/68081707:_____/18:00491232 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1002/celc.201800275" target="_blank" >http://dx.doi.org/10.1002/celc.201800275</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/celc.201800275" target="_blank" >10.1002/celc.201800275</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Modification of a Mercury Electrode with Different Thioalkanes: Structure-Sensitive Bovine Serum Albumin Analysis

Popis výsledku v původním jazyce

Chronopotentiometric stripping (CPS) in combination with mercury electrodes is convenient for structure-sensitive protein analysis. By using this method, we tested the discrimination between native and denatured bovine serum albumin (BSA) at various alkanethiol self-assembled monolayers (SAMs). Our results showed that alkanethiol SAMs with different headgroups or different chain lengths had different influences on the efficiency of CPS in protecting BSA from the electric field-induced denaturation. SAMs with longer alkanethiol chain lengths were more efficient in protecting BSA from denaturation at negatively charged electrode surface than those formed by short-chain alkanethiols. Short alkanethiol SAMs could be prepared by co-adsorption with the protein on the electrode surface, which was not possible with the long-chain alkanethiols. CPS data were supported by impedance analysis. We believe that our work will be useful in the electrochemical sensing of nucleic acid-protein and protein-protein binding.

Název v anglickém jazyce

Modification of a Mercury Electrode with Different Thioalkanes: Structure-Sensitive Bovine Serum Albumin Analysis

Popis výsledku anglicky

Chronopotentiometric stripping (CPS) in combination with mercury electrodes is convenient for structure-sensitive protein analysis. By using this method, we tested the discrimination between native and denatured bovine serum albumin (BSA) at various alkanethiol self-assembled monolayers (SAMs). Our results showed that alkanethiol SAMs with different headgroups or different chain lengths had different influences on the efficiency of CPS in protecting BSA from the electric field-induced denaturation. SAMs with longer alkanethiol chain lengths were more efficient in protecting BSA from denaturation at negatively charged electrode surface than those formed by short-chain alkanethiols. Short alkanethiol SAMs could be prepared by co-adsorption with the protein on the electrode surface, which was not possible with the long-chain alkanethiols. CPS data were supported by impedance analysis. We believe that our work will be useful in the electrochemical sensing of nucleic acid-protein and protein-protein binding.

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

<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

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

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

ChemElectroChem

ISSN

2196-0216

e-ISSN

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Svazek periodika

5

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

7

Strana od-do

1373-1379

Kód UT WoS článku

000431974500006

EID výsledku v databázi Scopus

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