- Electrochemical sensing of tumor suppressor protein p53-deoxyribonucl…
Počet záznamů: 1  

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

  1. 1.
    SYSNO ASEP0435478
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleElectrochemical sensing of tumor suppressor protein p53-deoxyribonucleic acid complex stability at an electrified interface
    Author(s) Paleček, Emil (BFU-R) RID, ORCID
    Černocká, Hana (BFU-R) RID, ORCID
    Ostatná, Veronika (BFU-R) RID, ORCID
    Navrátilová, Lucie (BFU-R)
    Brázdová, Marie (BFU-R) RID, ORCID
    Number of authors5
    Source TitleAnalytica Chimica Acta. - : Elsevier - ISSN 0003-2670
    Roč. 828, MAY2014 (2014), s. 1-8
    Number of pages9 s.
    Publication formPrint - P
    Languageeng - English
    CountryNL - Netherlands
    KeywordsDeoxyribonucleic acid-protein binding ; Tumor suppressor protein p53 ; Electrochemical sensing
    Subject RIVBO - Biophysics
    R&D ProjectsGAP301/11/2055 GA ČR - Czech Science Foundation (CSF)
    GA13-00956S GA ČR - Czech Science Foundation (CSF)
    GA13-36108S GA ČR - Czech Science Foundation (CSF)
    Institutional supportBFU-R - RVO:68081707
    UT WOS000336336900001
    DOI https://doi.org/10.1016/j.aca.2014.03.029
    AnnotationElectrochemical 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 analysis of 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 between half-sites of the DNA consensus sequence.
    WorkplaceInstitute of Biophysics
    ContactJana Poláková, polakova@ibp.cz, Tel.: 541 517 244
    Year of Publishing2015
Počet záznamů: 1  

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