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Chronopotentiometry as a sensitive interfacial characterisation tool for peptide aptamer monolayers

par Ilimbi, Diane;Buess Herman, Claudine ;Doneux, Thomas
Référence Electroanalysis, 31, page (2041-2047)
Publication Publié, 2019-10-01

Article révisé par les pairs

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Résumé :

Constant current chronopotentiometry is employed in conjunction with cyclic voltammetry and ac voltammetry to present in-depth interfacial characterisations of the adsorption behaviour of a peptide affinity probe (Cys-p53), of a thiolated hepta(ethylene glycol) (t-OEG) and of mixed monolayers of these at mercury electrodes. The peptide sequence is derived from the interaction site of the protein p53 with the protein Mdm2. The adsorbed Cys-p53 peptide is catalytically active towards the hydrogen evolution reaction, giving rise to very intense peaks in chronopotentiometry, whereas the oligo(ethylene glycol) is not. This difference enables one to monitor the presence of the peptide within mixed monolayers. It is shown that in the binary layers, the adsorption of t-OEG is kinetically favoured while Cys-p53 is thermodynamically more strongly adsorbed.