Electrochemical detection of different p53 conformations by using nanostructured surfaces.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
22 11 2019
Historique:
received: 07 04 2019
accepted: 07 11 2019
entrez: 24 11 2019
pubmed: 24 11 2019
medline: 4 11 2020
Statut: epublish

Résumé

Protein electrochemistry represents a powerful technique for investigating the function and structure of proteins. Currently available biochemical assays provide limited information related to the conformational state of proteins and high costs. This work provides novel insights into the electrochemical investigation of the metalloprotein p53 and its redox products using label-free direct electrochemistry and label-based antibody-specific approaches. First, the redox activities of different p53 redox products were qualitatively investigated on carbon-based electrodes. Then, focusing on the open p53 isoform (denatured p53), a quantitative analysis was performed, comparing the performances of different bulk and nanostructured materials (carbon and platinum). Overall, four different p53 products could be successfully discriminated, from wild type to denatured. Label-free analysis suggested a single electron exchange with electron transfer rate constants on the order of 1 s

Identifiants

pubmed: 31758050
doi: 10.1038/s41598-019-53994-6
pii: 10.1038/s41598-019-53994-6
pmc: PMC6874615
doi:

Substances chimiques

Antibodies 0
TP53 protein, human 0
Tumor Suppressor Protein p53 0
Platinum 49DFR088MY
Carbon 7440-44-0
Gold 7440-57-5

Types de publication

Comparative Study Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

17347

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Auteurs

Sarah Tonello (S)

Department of Information Engineering, University of Brescia, Brescia, Italy. s.tonello@unibs.it.

Francesca Stradolini (F)

Integrated Systems Laboratory (LSI), EPFL, Lausanne, Switzerland.

Giulia Abate (G)

Department of Molecular and Translational Medicine, University of Brescia, Brescia, Italy.

Daniela Uberti (D)

Department of Molecular and Translational Medicine, University of Brescia, Brescia, Italy.

Mauro Serpelloni (M)

Department of Information Engineering, University of Brescia, Brescia, Italy.

Sandro Carrara (S)

Integrated Systems Laboratory (LSI), EPFL, Lausanne, Switzerland.

Emilio Sardini (E)

Department of Information Engineering, University of Brescia, Brescia, Italy.

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Classifications MeSH