Electrochemical oxidation of proteins using ionic liquids as solubilizers, adsorption solvents and electrolytes

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F14%3A33148910" target="_blank" >RIV/61989592:15310/14:33148910 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61989592:15110/14:33148910

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.electacta.2013.06.115" target="_blank" >http://dx.doi.org/10.1016/j.electacta.2013.06.115</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.electacta.2013.06.115" target="_blank" >10.1016/j.electacta.2013.06.115</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Electrochemical oxidation of proteins using ionic liquids as solubilizers, adsorption solvents and electrolytes

Popis výsledku v původním jazyce

This study focuses on application of room temperature ionic liquids (RTILs) as solubilizers, adsorption solvents and supporting electrolytes for electrochemical analysis of human and bovine serum albumins, HSA and BSA. The proteins were analyzed by ex situ, adsorptive transfer, square-wave voltammetry (SWV) at a basal-plane pyrolytic graphite electrode after solubilization using imidazolium- and ammonium-based RTILs. The application of RTILs enabled SWV scan from 0 to +1.5 V (vs. Ag/AgCl/3 M KCl) without interference with the anodic response of the proteins. Concretely, Tyr (Y) and Trp (W) oxidation currentsof HSA and BSA, peak Y&W around +0.85 V, were observed and characterized under different RTILs and RTIL/water conditions. The electrochemical datawere supported by electrophoresis under denaturing and native conditions. These provided evidence for the structural changes and stability of the studied proteinsin the presence of RTILs. The data acquired using BSA and HSA model proteins

Název v anglickém jazyce

Electrochemical oxidation of proteins using ionic liquids as solubilizers, adsorption solvents and electrolytes

Popis výsledku anglicky

This study focuses on application of room temperature ionic liquids (RTILs) as solubilizers, adsorption solvents and supporting electrolytes for electrochemical analysis of human and bovine serum albumins, HSA and BSA. The proteins were analyzed by ex situ, adsorptive transfer, square-wave voltammetry (SWV) at a basal-plane pyrolytic graphite electrode after solubilization using imidazolium- and ammonium-based RTILs. The application of RTILs enabled SWV scan from 0 to +1.5 V (vs. Ag/AgCl/3 M KCl) without interference with the anodic response of the proteins. Concretely, Tyr (Y) and Trp (W) oxidation currentsof HSA and BSA, peak Y&W around +0.85 V, were observed and characterized under different RTILs and RTIL/water conditions. The electrochemical datawere supported by electrophoresis under denaturing and native conditions. These provided evidence for the structural changes and stability of the studied proteinsin the presence of RTILs. The data acquired using BSA and HSA model proteins

Druh

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

CEP obor

CG - Elektrochemie

OECD FORD obor

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Projekt

<a href="/cs/project/EE2.3.20.0057" target="_blank" >EE2.3.20.0057: Rozvoj a internacionalizace biofyzikálního výzkumu na Přírodovědecké fakultě Univerzity Palackého v Olomouci</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

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

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Svazek periodika

126

Číslo periodika v rámci svazku

April

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

6

Strana od-do

31-36

Kód UT WoS článku

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EID výsledku v databázi Scopus

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