Chronopotentiometric Analysis of Proteins at Charged Electrode Surfaces

0511687 - BFÚ 2020 RIV DE eng J - Článek v odborném periodiku
Melnikova, E. - Izadi, Nasim - Gál, M. - Ostatná, Veronika
Chronopotentiometric Analysis of Proteins at Charged Electrode Surfaces.
Electroanalysis. Roč. 31, č. 10 (2019), s. 1868-1872. ISSN 1040-0397. E-ISSN 1521-4109
Institucionální podpora: RVO:68081707
Klíčová slova: bovine serum-albumin * hydrogen evolution * mercury * polylysine * catalysis * Catalytic hydrogen evolution reaction
Obor OECD: Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)
Impakt faktor: 2.544, rok: 2019
Způsob publikování: Omezený přístup
https://onlinelibrary.wiley.com/doi/full/10.1002/elan.201900239

Protein properties and functions are strongly dependent on the structure and amino acid content. In this work, catalytic hydrogen evolution reaction (CHER) of five proteins (human serum albumin, lysozyme, beta-synuclein, H2 A and H3 histones) were studied using constant current chronopotentiometric stripping (CPS) with the aim to find out the association between protein content and its electrochemical response. We have shown that the height and potential of CPS peak H in dependence on accumulation potential differed for the studied proteins, while the CPS peak area was almost the same for all of them. CV and CPS peaks H of Cys-containing proteins appeared at less negative potentials in comparison to proteins without Cys, suggesting easier CHER. Acidic and basic proteins not containing Cys can be also recognized due to their different CPS response after their adsorption at the positive and negative charged interface.
Trvalý link: http://hdl.handle.net/11104/0301907