Ion-transfer voltammetric behavior of protein digests at liquid|liquid interfaces

Grégoire Herzog, Amandine Roger, David Sheehan, Damien W.M. Arrigan

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


The development of new methods for the detection of proteins and peptides is of widespread importance. In this work, the electrochemical behavior of peptide mixtures resulting from proteolytic digestion of proteins was investigated at the polarized liquid|liquid interface (or the interface between two immiscible electrolyte solutions, ITIES). The influence of pepsin digestion on three proteins (hemoglobin, lysozyme, and cytochrome c) was studied, and it was revealed that resulting cyclic voltammograms of the three protein digests were different due to the unique peptide mixtures for a given protein. Differential pulse stripping voltammetry of protein digests enabled the detection of digested proteins at concentrations ranging between 0.55 and 4.22 μM. A limit of detection of 0.55 μM of the initial concentration of protein was achieved, demonstrating the analytical possibilities of such an electrochemical method. These results show that iontransfer voltammetry offers the opportunity to study and develop label-free detection of peptides resulting from enzymatic digestions of proteins and may thus have a role in development of new proteomic technologies.

Original languageBritish English
Pages (from-to)258-264
Number of pages7
JournalAnalytical Chemistry
Issue number1
StatePublished - 2010


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