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Lable-free electrochemical analysis of biomacromolecules

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F17%3A00486104" target="_blank" >RIV/68081707:_____/17:00486104 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.apmt.2017.08.011" target="_blank" >http://dx.doi.org/10.1016/j.apmt.2017.08.011</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.apmt.2017.08.011" target="_blank" >10.1016/j.apmt.2017.08.011</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Lable-free electrochemical analysis of biomacromolecules

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10405 - Electrochemistry (dry cells, batteries, fuel cells, corrosion metals, electrolysis)

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2017

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Applied Materials Today

  • ISSN

    2352-9407

  • e-ISSN

  • Volume of the periodical

    9

  • Issue of the periodical within the volume

    2017

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    17

  • Pages from-to

    434-450

  • UT code for WoS article

    000417805400047

  • EID of the result in the Scopus database