About: Electrochemical oxidation of proteins using ionic liquids as solubilizers, adsorption solvents and electrolytes     Goto   Sponge   NotDistinct   Permalink

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  • This study focuses on application of room temperature ionic liquids (RTILs) as solubilizers, adsorption solvents and supporting electrolytes for electrochemical analysis of human and bovine serum albumins, HSA and BSA. The proteins were analyzed by ex situ, adsorptive transfer, square-wave voltammetry (SWV) at a basal-plane pyrolytic graphite electrode after solubilization using imidazolium- and ammonium-based RTILs. The application of RTILs enabled SWV scan from 0 to +1.5 V (vs. Ag/AgCl/3 M KCl) without interference with the anodic response of the proteins. Concretely, Tyr (Y) and Trp (W) oxidation currentsof HSA and BSA, peak Y&W around +0.85 V, were observed and characterized under different RTILs and RTIL/water conditions. The electrochemical data were supported by electrophoresis under denaturing and native conditions. These provided evidence for the structural changes and stability of the studied proteinsin the presence of RTILs. The data acquired using BSA and HSA model proteins, could be used in further applications of RTILs in protein electrochemistry and for developing new protein sensing strategies.
  • This study focuses on application of room temperature ionic liquids (RTILs) as solubilizers, adsorption solvents and supporting electrolytes for electrochemical analysis of human and bovine serum albumins, HSA and BSA. The proteins were analyzed by ex situ, adsorptive transfer, square-wave voltammetry (SWV) at a basal-plane pyrolytic graphite electrode after solubilization using imidazolium- and ammonium-based RTILs. The application of RTILs enabled SWV scan from 0 to +1.5 V (vs. Ag/AgCl/3 M KCl) without interference with the anodic response of the proteins. Concretely, Tyr (Y) and Trp (W) oxidation currentsof HSA and BSA, peak Y&W around +0.85 V, were observed and characterized under different RTILs and RTIL/water conditions. The electrochemical data were supported by electrophoresis under denaturing and native conditions. These provided evidence for the structural changes and stability of the studied proteinsin the presence of RTILs. The data acquired using BSA and HSA model proteins, could be used in further applications of RTILs in protein electrochemistry and for developing new protein sensing strategies. (en)
Title
  • Electrochemical oxidation of proteins using ionic liquids as solubilizers, adsorption solvents and electrolytes
  • Electrochemical oxidation of proteins using ionic liquids as solubilizers, adsorption solvents and electrolytes (en)
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  • Electrochemical oxidation of proteins using ionic liquids as solubilizers, adsorption solvents and electrolytes
  • Electrochemical oxidation of proteins using ionic liquids as solubilizers, adsorption solvents and electrolytes (en)
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  • RIV/61989592:15110/14:33148910!RIV15-MSM-15110___
http://linked.open...avai/riv/aktivita
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  • I, P(EE2.3.20.0057)
http://linked.open...iv/cisloPeriodika
  • April
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  • 14114
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  • RIV/61989592:15110/14:33148910
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  • Electrolytes; Protein stability; Electrochemical sensing; Ionic liquid; Protein (en)
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  • GB - Spojené království Velké Británie a Severního Irska
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  • [FAEC2C160ED3]
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  • Electrochimica Acta
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  • 126
http://linked.open...iv/tvurceVysledku
  • Vacek, Jan
  • Kubala, Martin
  • Vrba, Jiří
  • Zatloukalová, Martina
issn
  • 0013-4686
number of pages
http://bibframe.org/vocab/doi
  • 10.1016/j.electacta.2013.06.115
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  • 15110
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