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

J 2021

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

PAVELICOVA, Kristyna; Lucie VANICKOVA; Yazan HADDAD; Lukas NEJDL; Jan ZITKA et al.

Základní údaje

Originální název

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

Autoři

PAVELICOVA, Kristyna; Lucie VANICKOVA; Yazan HADDAD; Lukas NEJDL; Jan ZITKA; Silvia KOCIOVA; Filip MRAVEC; Tomáš VACULOVIČ; Mirek MACKA; Marketa VACULOVICOVA a Vojtech ADAM

Vydání

International Journal of Biological Macromolecules, Elsevier B.V. 2021, 0141-8130

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10601 Cell biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 8.025

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/21:00121520

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

FRET; Quantum dots; Oligomerization; Capillary electrophoresis

Štítky

14313010, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 3. 5. 2021 16:22, Mgr. Marie Novosadová Šípková, DiS.

Anotace

V originále

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.

Návaznosti

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

Citovat

PAVELICOVA, Kristyna; Lucie VANICKOVA; Yazan HADDAD; Lukas NEJDL; Jan ZITKA; Silvia KOCIOVA; Filip MRAVEC; Tomáš VACULOVIČ; Mirek MACKA; Marketa VACULOVICOVA a Vojtech ADAM. Metallothionein dimerization evidenced by QD-based Forster resonance energy transfer and capillary electrophoresis. International Journal of Biological Macromolecules. Elsevier B.V., 2021, roč. 170, February, s. 53-60. ISSN 0141-8130. Dostupné z: https://doi.org/10.1016/j.ijbiomac.2020.12.105.

@article{1765378,
   author = {Pavelicova, Kristyna and Vanickova, Lucie and Haddad, Yazan and Nejdl, Lukas and Zitka, Jan and Kociova, Silvia and Mravec, Filip and Vaculovič, Tomáš and Macka, Mirek and Vaculovicova, Marketa and Adam, Vojtech},
   article_number = {February},
   doi = {https://doi.org/10.1016/j.ijbiomac.2020.12.105},
   keywords = {FRET; Quantum dots; Oligomerization; Capillary electrophoresis},
   language = {eng},
   issn = {0141-8130},
   journal = {International Journal of Biological Macromolecules},
   title = {Metallothionein dimerization evidenced by QD-based Forster resonance energy transfer and capillary electrophoresis},
   url = {https://doi.org/10.1016/j.ijbiomac.2020.12.105},
   volume = {170},
   year = {2021}
}

TY  - JOUR
ID  - 1765378
AU  - Pavelicova, Kristyna - Vanickova, Lucie - Haddad, Yazan - Nejdl, Lukas - Zitka, Jan - Kociova, Silvia - Mravec, Filip - Vaculovič, Tomáš - Macka, Mirek - Vaculovicova, Marketa - Adam, Vojtech
PY  - 2021
TI  - Metallothionein dimerization evidenced by QD-based Forster resonance energy transfer and capillary electrophoresis
JF  - International Journal of Biological Macromolecules
VL  - 170
IS  - February
SP  - 53-60
EP  - 53-60
PB  - Elsevier B.V.
SN  - 01418130
KW  - FRET
KW  - Quantum dots
KW  - Oligomerization
KW  - Capillary electrophoresis
UR  - https://doi.org/10.1016/j.ijbiomac.2020.12.105
N2  - 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.
ER  -

PAVELICOVA, Kristyna; Lucie VANICKOVA; Yazan HADDAD; Lukas NEJDL; Jan ZITKA; Silvia KOCIOVA; Filip MRAVEC; Tomáš VACULOVIČ; Mirek MACKA; Marketa VACULOVICOVA a Vojtech ADAM. Metallothionein dimerization evidenced by QD-based Forster resonance energy transfer and capillary electrophoresis. \textit{International Journal of Biological Macromolecules}. Elsevier B.V., 2021, roč.~170, February, s.~53-60. ISSN~0141-8130. Dostupné z: https://doi.org/10.1016/j.ijbiomac.2020.12.105.

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