About: Electrochemical sensing of tumor suppressor protein p53-deoxyribonucleic acid complex stability at an electrified interface     Goto   Sponge   NotDistinct   Permalink

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  • 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 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.
  • 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 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. (en)
Title
  • Electrochemical sensing of tumor suppressor protein p53-deoxyribonucleic acid complex stability at an electrified interface
  • Electrochemical sensing of tumor suppressor protein p53-deoxyribonucleic acid complex stability at an electrified interface (en)
skos:prefLabel
  • Electrochemical sensing of tumor suppressor protein p53-deoxyribonucleic acid complex stability at an electrified interface
  • Electrochemical sensing of tumor suppressor protein p53-deoxyribonucleic acid complex stability at an electrified interface (en)
skos:notation
  • RIV/68081707:_____/14:00435478!RIV15-GA0-68081707
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • I, P(GA13-00956S), P(GA13-36108S), P(GAP301/11/2055), P(GBP305/12/G034)
http://linked.open...iv/cisloPeriodika
  • MAY2014
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
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  • 14117
http://linked.open...ai/riv/idVysledku
  • RIV/68081707:_____/14:00435478
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Deoxyribonucleic acid-protein binding; Tumor suppressor protein p53; Electrochemical sensing (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • NL - Nizozemsko
http://linked.open...ontrolniKodProRIV
  • [2DD39D433992]
http://linked.open...i/riv/nazevZdroje
  • Analytica Chimica Acta
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 828
http://linked.open...iv/tvurceVysledku
  • Brázdová, Marie
  • Navrátilová, Lucie
  • Ostatná, Veronika
  • Paleček, Emil
  • Černocká, Hana
http://linked.open...ain/vavai/riv/wos
  • 000336336900001
issn
  • 0003-2670
number of pages
http://bibframe.org/vocab/doi
  • 10.1016/j.aca.2014.03.029
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