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Highly stable enzyme-mimicking nanocomposite of antioxidant activity. | LitMetric

Highly stable enzyme-mimicking nanocomposite of antioxidant activity.

J Colloid Interface Sci

MTA-SZTE Lendület Biocolloids Research Group, University of Szeged, H-6720 Szeged, Hungary; Interdisciplinary Excellence Center, Department of Physical Chemistry and Materials Science, University of Szeged, H-6720 Szeged, Hungary. Electronic address:

Published: May 2019

AI Article Synopsis

  • A stable nanocomposite with antioxidant properties was created by binding a metal complex that mimics superoxide dismutase to treated nanoclay.
  • Surface modification was achieved using a specific copolymer that enhanced the stability of the nanocomposite in solutions with high salt concentrations.
  • This new hybrid showed improved scavenging activity for harmful superoxide radicals compared to the original metal complex and maintained its effectiveness better than traditional antioxidant enzymes under heat and electrolyte stress.

Article Abstract

A highly stable nanocomposite of antioxidant activity was developed by immobilization of a superoxide dismutase-mimicking metal complex on copolymer-functionalized nanoclay. The layered double hydroxide (LDH) nanoclays were synthesized and surface modification was performed by adsorbing poly(vinylpyridine-b-methacrylic acid) (PVPMAA). The effect of the adsorption on the charging and aggregation properties was investigated and the copolymer dose was optimized to obtain stable LDH dispersions. The LDH-PVPMAA hybrid particles showed high resistance against salt-induced destabilization in aqueous dispersions. Copper(II)-histamine (Cu(Hsm)) complexes were immobilized via the formation of dative bonds between the metal ions and the nitrogen atoms of the functional groups of the copolymer adsorbed on the particles. Changes in the coordination geometry of the complex upon immobilization led to higher superoxide radical anion scavenging activity than the one determined for the non-immobilized complex. Comparison of superoxide dismutase (SOD)-like activity of the obtained hybrid LDH-PVPMAA-Cu(Hsm) with the nanoclay-immobilized SOD enzyme revealed that the developed composite maintained its activity over several days and was able to function at elevated temperature, while the immobilized native enzyme lost its activity under these experimental conditions. The developed nanocomposite is a promising antioxidant candidate in applications, where high electrolyte concentration and elevated temperature are applied.

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Source
http://dx.doi.org/10.1016/j.jcis.2019.02.050DOI Listing

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