Electrochemical data on redox properties of human Cofilin-2 and its Mutant S3D
Marcello Pignataro,
Giulia Di Rocco,
Lidia Lancellotti,
Fabrizio Bernini,
Khaushik Subramanian,
Elena Castellini,
Carlo Augusto Bortolotti,
Daniele Malferrari,
Daniele Moro,
Giovanni Valdrè,
Marco Borsari,
Federica del Monte
Affiliations
Marcello Pignataro
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, USA
Giulia Di Rocco
Department of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy
Lidia Lancellotti
Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Modena, Italy
Fabrizio Bernini
Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Modena, Italy
Khaushik Subramanian
Novartis Institutes of Biomedical Research, Boston, USA
Elena Castellini
Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Modena, Italy
Carlo Augusto Bortolotti
Department of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy
Daniele Malferrari
Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Modena, Italy
Daniele Moro
Department of Biological, Geological and Environmental Sciences, University of Bologna, Bologna, Italy
Giovanni Valdrè
Department of Biological, Geological and Environmental Sciences, University of Bologna, Bologna, Italy
Marco Borsari
Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, Modena, Italy; Corresponding authors.
Federica del Monte
Gazes Cardiac Research Institute, Medical University of South Carolina, Charleston, USA; Department of Experimental, Diagnostic and Specialty Medicine (DIMES), School of Medicine, University of Bologna, Bologna, Italy; Corresponding authors.
The reported data are related to a research paper entitled ''Phosphorylated cofilin-2 is more prone to oxidative modifications on Cys39 and favors amyloid fibril formation'' [1]. Info about the formation and redox properties of the disulfide bridge of a protein is quite difficult to obtain and only in a few cases was it possible to observe a cyclic voltammetry (CV) signal [2,3]. Human cofilin-2 contains two cysteines (Cys39 and Cys80) which can be oxidized in suitable conditions and form a disulfide bridge [1]. For this purpose, CV measurements were carried out on human cofilin-2 WT and its mutant S3D immobilized on a gold electrode coated by an anionic self-assembled monolayer (SAM), after a pre-oxidation time which was fundamental for observing a CV signal relating to the oxidation/reduction process of the disulfide bridge of the proteins. The data include CV curves obtained with and without electrochemical pre-oxidation and after oxidation with H2O2. In addition, the plot of the cathodic peak current vs. electrochemical pre-oxidation time and the pH dependence of the formal potential (E°’) are reported. The data obtained by CV measurements were used to determine the time required to form the disulfide bridge for the immobilized proteins and, consequently, to observe the CV signal, to calculate the E°’ values and analyse the pH dependence of E°’. The electrochemical data were provided which will be useful for further electrochemical investigations regarding proteins bearing disulfide bridge(s) or cysteines prone to oxidation.
