Label-free electrochemical detection of singlet oxygen protein damage

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F16%3A00456295" target="_blank" >RIV/68081707:_____/16:00456295 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.electacta.2015.11.104" target="_blank" >http://dx.doi.org/10.1016/j.electacta.2015.11.104</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.electacta.2015.11.104" target="_blank" >10.1016/j.electacta.2015.11.104</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Label-free electrochemical detection of singlet oxygen protein damage

Popis výsledku v původním jazyce

Oxidative damage of proteins results in changes of their structures and functions. In this work, the singlet oxygen (O-1(2))-mediated oxidation of bovine serum albumin (BSA) and urease by blue-light photosensitization of the tris(2,2'-bipyridine)ruthenium(II) cation [Ru(bpy)(3)](2+) was studied by square wave voltammetry at glassy carbon electrode and by constant current chronopotentiometry at mercury electrode. Small changes in voltammetric oxidation Tyr and Trp peaks did not indicate significant changes in the BSA structure after photo-oxidation at carbon electrode. On the other hand chronopotentiometric peak H of BSA at HMDE increased during blue-light photosensitization, indicating that photo-oxidized BSA was more susceptible to the electric field-induced denaturation than non-oxidized native BSA. Similar results were obtained for urease, where enzymatic activity was also evaluated. The present results show the capability of label- and reagent-free electrochemical methods to detect

Název v anglickém jazyce

Label-free electrochemical detection of singlet oxygen protein damage

Popis výsledku anglicky

Oxidative damage of proteins results in changes of their structures and functions. In this work, the singlet oxygen (O-1(2))-mediated oxidation of bovine serum albumin (BSA) and urease by blue-light photosensitization of the tris(2,2'-bipyridine)ruthenium(II) cation [Ru(bpy)(3)](2+) was studied by square wave voltammetry at glassy carbon electrode and by constant current chronopotentiometry at mercury electrode. Small changes in voltammetric oxidation Tyr and Trp peaks did not indicate significant changes in the BSA structure after photo-oxidation at carbon electrode. On the other hand chronopotentiometric peak H of BSA at HMDE increased during blue-light photosensitization, indicating that photo-oxidized BSA was more susceptible to the electric field-induced denaturation than non-oxidized native BSA. Similar results were obtained for urease, where enzymatic activity was also evaluated. The present results show the capability of label- and reagent-free electrochemical methods to detect

Druh

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

CEP obor

BO - Biofyzika

OECD FORD obor

—

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

Electrochimica acta

ISSN

0013-4686

e-ISSN

—

Svazek periodika

187

Číslo periodika v rámci svazku

JAN 2016

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

8

Strana od-do

662-669

Kód UT WoS článku

000367235600077

EID výsledku v databázi Scopus

—