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Activity of CdTe Quantum-Dot-Tagged Superoxide Dismutase and Its Analysis in Capillary Electrophoresis
N. Zaręba, Ł. Lewandowski, D. Kunachowicz, R. Kizek, M. Kepinska
Language English Country Switzerland
Document type Journal Article
Grant support
SUB.D170.21.042
Uniwersytet Medyczny im. Piastów Slaskich we Wroclawiu
NLK
Free Medical Journals
from 2000
Freely Accessible Science Journals
from 2000
PubMed Central
from 2007
Europe PubMed Central
from 2007
ProQuest Central
from 2000-03-01
Open Access Digital Library
from 2000-01-01
Open Access Digital Library
from 2007-01-01
Health & Medicine (ProQuest)
from 2000-03-01
ROAD: Directory of Open Access Scholarly Resources
from 2000
PubMed
34200401
DOI
10.3390/ijms22116156
Knihovny.cz E-resources
- MeSH
- Electrophoresis, Capillary methods MeSH
- Fluorescence MeSH
- Spectrometry, Fluorescence MeSH
- Quantum Dots * MeSH
- Humans MeSH
- Nanoparticles chemistry MeSH
- Cadmium Compounds chemistry MeSH
- Superoxide Dismutase analysis metabolism MeSH
- Tellurium chemistry MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
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.
References provided by Crossref.org
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