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Metallothionein dimerization evidenced by QD-based Förster resonance energy transfer and capillary electrophoresis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216305%3A26310%2F21%3APU138262" target="_blank" >RIV/00216305:26310/21:PU138262 - isvavai.cz</a>

  • Alternative codes found

    RIV/62156489:43210/21:43918913 RIV/00216224:14310/21:00121520

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/pii/S0141813020352466?via=ihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813020352466?via=ihub</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.ijbiomac.2020.12.105" target="_blank" >10.1016/j.ijbiomac.2020.12.105</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Metallothionein dimerization evidenced by QD-based Förster resonance energy transfer and capillary electrophoresis

  • Original language description

    Herein, we report a new simple and easy-to-use approach for the characterization of protein oligomerization based on fluorescence resonance energy transfer (FRET) and capillary electrophoresis with LED-induced detection. The FRET pair consisted of quantum dots (QDs) used as an emission tunable donor (emission wavelength of 450 nm) and a cyanine dye (Cy3), providing optimal optical properties as an acceptor. Nonoxidative dimerization of mammalian metallothionein (MT) was investigated using the donor and acceptor covalently conjugated to MT. The main functions of MTs within an organism include the transport and storage of essential metal ions and detoxification of toxic ions. Upon storage under aerobic conditions, MTs form dimers (as well as higher oligomers), which may play an essential role as mediators in oxidoreduction signaling pathways. Due to metal bridging by Cd2+ ions between molecules of metallothionein, the QDs and Cy3 were close enough, enabling a FRET signal. The FRET efficiency was calculated to be in the range of 11–77%. The formation of MT dimers in the presence of Cd2+ ions was confirmed by MALDI-MS analyses. Finally, the process of oligomerization resulting in FRET was monitored by CE, and oligomerization of MT was confirmed.

  • 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

    10406 - Analytical chemistry

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)<br>S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

  • ISSN

    0141-8130

  • e-ISSN

    1879-0003

  • Volume of the periodical

    170

  • Issue of the periodical within the volume

    2021

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    8

  • Pages from-to

    53-60

  • UT code for WoS article

    000613921400006

  • EID of the result in the Scopus database

    2-s2.0-85098131107