Pignataro Marcello, Rocco Giulia Di, Lancellotti Lidia, Bernini Fabrizio, Subramanian Khaushik, Castellini Elena, Bortolotti Carlo Augusto, Malferrari Daniele, Moro Daniele, Valdrè Giovanni, Borsari Marco, Monte Federica Del
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, USA.
Department of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Data Brief. 2020 Sep 24;33:106345. doi: 10.1016/j.dib.2020.106345. eCollection 2020 Dec.
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 HO. In addition, the plot of the cathodic peak current 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.
所报道的数据与一篇题为《磷酸化的丝切蛋白-2在半胱氨酸39处更易于发生氧化修饰并有利于淀粉样纤维形成》的研究论文相关[1]。关于蛋白质二硫键的形成和氧化还原性质的信息很难获得，只有在少数情况下才有可能观察到循环伏安法（CV）信号[2,3]。人丝切蛋白-2含有两个半胱氨酸（半胱氨酸39和半胱氨酸80），在合适的条件下它们可以被氧化并形成二硫键[1]。为此，在经过一段预氧化时间后，对固定在由阴离子自组装单层（SAM）包覆的金电极上的人丝切蛋白-2野生型及其突变体S3D进行了CV测量，这段预氧化时间对于观察与蛋白质二硫键氧化/还原过程相关的CV信号至关重要。数据包括在有和没有电化学预氧化以及用过氧化氢氧化之后获得的CV曲线。此外，还报告了阴极峰电流与电化学预氧化时间的关系图以及形式电位（E°'）的pH依赖性。通过CV测量获得的数据用于确定固定化蛋白质形成二硫键所需的时间，从而观察CV信号，计算E°'值并分析E°'的pH依赖性。提供了电化学数据，这将有助于进一步开展关于带有二硫键或易于氧化的半胱氨酸的蛋白质的电化学研究。
