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Lable-free electrochemical analysis of biomacromolecules
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SYSNO ASEP 0486104 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Lable-free electrochemical analysis of biomacromolecules Author(s) Paleček, Emil (BFU-R) RID, ORCID
Dorčák, Vlastimil (BFU-R) RID, ORCIDNumber of authors 2 Source Title Applied Materials Today. - : Elsevier - ISSN 2352-9407
Roč. 9, č. 2017 (2017), s. 434-450Number of pages 17 s. Publication form Print - P Language eng - English Country NL - Netherlands Keywords carbon-paste electrodes ; pyrolytic-graphite electrode ; structure-sensitive analysis Subject RIV CG - Electrochemistry OECD category Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis) R&D Projects GA17-08971S GA ČR - Czech Science Foundation (CSF) GA15-15479S GA ČR - Czech Science Foundation (CSF) Institutional support BFU-R - RVO:68081707 UT WOS 000417805400047 DOI 10.1016/j.apmt.2017.08.011 Annotation Recent progress in label-free electrochemical analysis of biomacromolecules, such as proteins, nucleicacids and carbohydrates is reviewed. Since the 1970s electrochemical analysis of proteins focused on non-protein redox-active components of a relatively small group of conjugated proteins. In the recent decade, the ability of practically of all proteins to catalyze hydrogen evolution at mercury-containing electrodes was utilized for development of the protein structure-sensitive analysis. Some amino acid residues, such as arginine, lysine and cysteine contribute to the catalytic hydrogen evolution reaction (CHER) at neutral pH yielding protein reduction signals at highly negative potentials. It was found that native proteins do not lose their folded structure when adsorbed at mercury electrode close to the potential of zero charge. Surface-attached proteins get however denatured due to the electric field effects during their prolonged exposure to negative potentials. Using the constant current chronopotentiometric stripping it was possible to limit the exposure time to milliseconds preventing protein denaturation. The method was utilized in detection of changes in protein structures due to mutation, chemical modification, aggregation, damage by environmental agents, as well as to studies of poorly soluble membrane proteins, DNA-protein and protein-protein interactions, etc. Application of voltammetric methods, such as fast scan CV and normal pulse voltammetry showed smaller sensitivity to tiny changes in protein structures. Recently CHER was found also in some polysaccharides such as chitosan and in NH2 group-containing glycans. Very recent development in electrochemical analysis of DNA and RNA was briefly summarized. (C) 2017 Elsevier Ltd. All rights reserved. Workplace Institute of Biophysics Contact Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244 Year of Publishing 2018
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