Electrochemical data on redox properties of human Cofilin-2 and its Mutant S3D

• Main Authors: 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
• Format: Article
• Language: English
• Published: Elsevier 2020-12-01
• Series: Data in Brief
• Subjects: Human cofilin; Disulfide bridge; Cyclic voltammetry; Redox properties; Electrochemistry; Cysteine
• Online Access: http://www.sciencedirect.com/science/article/pii/S2352340920312385

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.