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  Nanocomposite-based dual enzyme system for broad-spectrum scavenging of reactive oxygen species

Pavlovic, M., Muráth, S., Katona, X., Alsharif, N. B., Rouster, P., Maléth, J., et al. (2021). Nanocomposite-based dual enzyme system for broad-spectrum scavenging of reactive oxygen species. Scientific Reports, 11(1). doi:10.1038/s41598-021-83819-4.

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Pavlovic, Marko1, Author              
Muráth, Szabolcs, Author
Katona, Xénia, Author
Alsharif, Nizar B., Author
Rouster, Paul, Author
Maléth, József, Author
Szilagyi, Istvan, Author
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1Lukas Zeininger, Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_3179204              

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 Abstract: A broad-spectrum reactive oxygen species (ROS)-scavenging hybrid material (CASCADE) was developed by sequential adsorption of heparin (HEP) and poly(L-lysine) (PLL) polyelectrolytes together with superoxide dismutase (SOD) and horseradish peroxidase (HRP) antioxidant enzymes on layered double hydroxide (LDH) nanoclay support. The synthetic conditions were optimized so that CASCADE possessed remarkable structural (no enzyme leakage) and colloidal (excellent resistance against salt-induced aggregation) stability. The obtained composite was active in decomposition of both superoxide radical anions and hydrogen peroxide in biochemical assays revealing that the strong electrostatic interaction with the functionalized support led to high enzyme loadings, nevertheless, it did not interfere with the native enzyme conformation. In vitro tests demonstrated that ROS generated in human cervical adenocarcinoma cells were successfully consumed by the hybrid material. The cellular uptake was not accompanied with any toxicity effects, which makes the developed CASCADE a promising candidate for treatment of oxidative stress-related diseases.

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Language(s): eng - English
 Dates: 2021-02-222021
 Publication Status: Published in print
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 Identifiers: DOI: 10.1038/s41598-021-83819-4
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Title: Scientific Reports
  Abbreviation : Sci. Rep.
Source Genre: Journal
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Publ. Info: London, UK : Springer Nature
Pages: 4321 Volume / Issue: 11 (1) Sequence Number: - Start / End Page: - Identifier: ISSN: 2045-2322