ArticleRSC advances2020
Copper-tripeptides (cuzymes) with peroxidase-mimetic activity.
Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 12 citations in OpenAlex.
- Article
- Synergistic degradation of levofloxacin (LEV) by CuUltrasonics sonochemistry · 2025Article
- Progress in the Development of Biosensors Based on Peptide-Copper Coordination Interaction.Biosensors · 2022Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peroxidases are enzymes that use hydrogen peroxide to oxidize substrates such as 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ATBS). In this study, we showed that copper-tripeptide complexes ("cuzymes") also exhibited peroxidase-like activities. Different cuzymes could be formed by using various tripeptide ligands, such as GGG, GGH or HGG. However, the peroxidase-like activity of cuzymes depends on the sequence of the tripeptide (Cu-GGG > Cu-HGG > Cu-GGH). When ABTS was used as the substrate, the activity of Cu-GGG was 326 ± 1.5 U mg
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Registered trials
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