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

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