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

Varování

Publikace nespadá pod Filozofickou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.
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PAVELICOVA Kristyna VANICKOVA Lucie HADDAD Yazan NEJDL Lukas ZITKA Jan KOCIOVA Silvia MRAVEC Filip VACULOVIČ Tomáš MACKA Mirek VACULOVICOVA Marketa ADAM Vojtech

Rok publikování 2021
Druh Článek v odborném periodiku
Časopis / Zdroj International Journal of Biological Macromolecules
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
www https://doi.org/10.1016/j.ijbiomac.2020.12.105
Doi http://dx.doi.org/10.1016/j.ijbiomac.2020.12.105
Klíčová slova FRET; Quantum dots; Oligomerization; Capillary electrophoresis
Popis 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. (C) 2020 Elsevier B.V. All rights reserved.
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