Activity of CdTe Quantum-Dot-Tagged Superoxide Dismutase and Its Analysis in Capillary Electrophoresis

Autor: Natalia Zaręba, René Kizek, Dominika Kunachowicz, Łukasz Lewandowski, Marta Kepinska
Rok vydání: 2021
Předmět:
QH301-705.5
animal diseases
SOD1
capillary electrophoresis
Nanoparticle
02 engineering and technology
010402 general chemistry
01 natural sciences
Catalysis
Article
Fluorescence
Inorganic Chemistry
Superoxide dismutase
Capillary electrophoresis
Quantum Dots
Cadmium Compounds
Humans
Physical and Theoretical Chemistry
Biology (General)
Molecular Biology
QD1-999
Spectroscopy
chemistry.chemical_classification
biology
Superoxide Dismutase
Organic Chemistry
technology
industry
and agriculture
nutritional and metabolic diseases
Electrophoresis
Capillary
General Medicine
protein labeling
021001 nanoscience & nanotechnology
equipment and supplies
Enzyme assay
0104 chemical sciences
Computer Science Applications
nervous system diseases
enzyme activity
Chemistry
Enzyme
Spectrometry
Fluorescence
chemistry
Quantum dot
biology.protein
Biophysics
Nanoparticles
Tellurium
0210 nano-technology
Zdroj: International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 22, Iss 6156, p 6156 (2021)
Volume 22
Issue 11
ISSN: 1422-0067
Popis: Quantum dots (QDs) have a broad range of applications in cell biolabeling, cancer treatment, metastasis imaging, and therapeutic drug monitoring. Despite their wide use, relatively little is known about their influence on other molecules. Interactions between QDs and proteins can influence the properties of both nanoparticles and proteins. The effect of mercaptosuccinic acid-capped CdTe QDs on intercellular copper–zinc superoxide dismutase (SOD1)—one of the main enzymatic antioxidants—was investigated. Incubation of SOD1 with QDs caused an increase in SOD1 activity, unlike in the case of CdCl2, which inhibited SOD1. Moreover, this effect on SOD1 increased with the size and potential of QDs, although the effect became clearly visible in higher concentrations of QDs. The intensity of QD-SOD1 fluorescence, analyzed with the use of capillary electrophoresis with laser-induced fluorescence detection, was dependent on SOD1 concentration. In the case of green QDs, the fluorescence signal decreased with increasing SOD1 concentration. In contrast, the signal strength for Y-QD complexes was not dependent on SOD1 dilutions. The migration time of QDs and their complexes with SOD1 varied depending on the type of QD used. The migration time of G-QD complexes with SOD1 differed slightly. However, in the case of Y-QD complexes with SOD1, the differences in the migration time were not dependent on SOD concentration. This research shows that QDs interact with SOD1 and the influence of QDs on SOD activity is size-dependent. With this knowledge, one might be able to control the activation/inhibition of specific enzymes, such as SOD1.
Databáze: OpenAIRE
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