Electrochemical sensing of tumor suppressor protein p53-deoxyribonucleic acid complex stability at an electrified interface

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F14%3A00431786" target="_blank" >RIV/68081707:_____/14:00431786 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68081707:_____/14:00435478

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.aca.2014.03.029" target="_blank" >http://dx.doi.org/10.1016/j.aca.2014.03.029</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.aca.2014.03.029" target="_blank" >10.1016/j.aca.2014.03.029</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Electrochemical sensing of tumor suppressor protein p53-deoxyribonucleic acid complex stability at an electrified interface

Popis výsledku v původním jazyce

Electrochemical biosensors have the unique ability to convert biological events directly into electrical signals suitable for parallel analysis. Here we utilize specific properties of constant current chronopotentiometric stripping (CPS) in the analysisof protein and DNA-protein complex nanolayers. Rapid potential changes at high negative current intensities (I-str) in CPS are utilized in the analysis of DNA-protein interactions at thiol-modified mercury electrodes. P53 core domain (p53CD) sequence-specific binding to DNA results in a striking decrease in the electrocatalytic signal of free p53. This decrease is related to changes in the accessibility of the electroactive amino acid residues in the p53CD-DNA complex. By adjusting I-str and temperature, weaker non-specific binding can be eliminated or distinguished from the sequence-specific binding. The method also reflects differences in the stabilities of different sequence-specific complexes, including those containing spacers betw

Název v anglickém jazyce

Electrochemical sensing of tumor suppressor protein p53-deoxyribonucleic acid complex stability at an electrified interface

Popis výsledku anglicky

Electrochemical biosensors have the unique ability to convert biological events directly into electrical signals suitable for parallel analysis. Here we utilize specific properties of constant current chronopotentiometric stripping (CPS) in the analysisof protein and DNA-protein complex nanolayers. Rapid potential changes at high negative current intensities (I-str) in CPS are utilized in the analysis of DNA-protein interactions at thiol-modified mercury electrodes. P53 core domain (p53CD) sequence-specific binding to DNA results in a striking decrease in the electrocatalytic signal of free p53. This decrease is related to changes in the accessibility of the electroactive amino acid residues in the p53CD-DNA complex. By adjusting I-str and temperature, weaker non-specific binding can be eliminated or distinguished from the sequence-specific binding. The method also reflects differences in the stabilities of different sequence-specific complexes, including those containing spacers betw

Druh

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

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

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

Návaznosti

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

Analytica Chimica Acta

ISSN

0003-2670

e-ISSN

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Svazek periodika

828

Číslo periodika v rámci svazku

MAY2014

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

8

Strana od-do

1-8

Kód UT WoS článku

000336336900001

EID výsledku v databázi Scopus

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