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Protein Corona Hinders N-CQDs Oxidative Potential and Favors Their Application as Nanobiocatalytic System
The oxidative properties of nanomaterials arouse legitimate concerns about oxidative damage in biological systems. On the other hand, the undisputable benefits of nanomaterials promote them for biomedical applications; thus, the strategies to reduce oxidative potential are urgently needed. We aimed...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8347256/ https://www.ncbi.nlm.nih.gov/pubmed/34360901 http://dx.doi.org/10.3390/ijms22158136 |
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author | Czarnecka, Joanna Kwiatkowski, Mateusz Wiśniewski, Marek Roszek, Katarzyna |
author_facet | Czarnecka, Joanna Kwiatkowski, Mateusz Wiśniewski, Marek Roszek, Katarzyna |
author_sort | Czarnecka, Joanna |
collection | PubMed |
description | The oxidative properties of nanomaterials arouse legitimate concerns about oxidative damage in biological systems. On the other hand, the undisputable benefits of nanomaterials promote them for biomedical applications; thus, the strategies to reduce oxidative potential are urgently needed. We aimed at analysis of nitrogen-containing carbon quantum dots (N-CQDs) in terms of their biocompatibility and internalization by different cells. Surprisingly, N-CQD uptake does not contribute to the increased oxidative stress inside cells and lacks cytotoxic influence even at high concentrations, primarily through protein corona formation. We proved experimentally that the protein coating effectively limits the oxidative capacity of N-CQDs. Thus, N-CQDs served as an immobilization support for three different enzymes with the potential to be used as therapeutics. Various kinetic parameters of immobilized enzymes were analyzed. Regardless of the enzyme structure and type of reaction catalyzed, adsorption on the nanocarrier resulted in increased catalytic efficiency. The enzymatic-protein-to-nanomaterial ratio is the pivotal factor determining the course of kinetic parameter changes that can be tailored for enzyme application. We conclude that the above properties of N-CQDs make them an ideal support for enzymatic drugs required for multiple biomedical applications, including personalized medical therapies. |
format | Online Article Text |
id | pubmed-8347256 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-83472562021-08-08 Protein Corona Hinders N-CQDs Oxidative Potential and Favors Their Application as Nanobiocatalytic System Czarnecka, Joanna Kwiatkowski, Mateusz Wiśniewski, Marek Roszek, Katarzyna Int J Mol Sci Article The oxidative properties of nanomaterials arouse legitimate concerns about oxidative damage in biological systems. On the other hand, the undisputable benefits of nanomaterials promote them for biomedical applications; thus, the strategies to reduce oxidative potential are urgently needed. We aimed at analysis of nitrogen-containing carbon quantum dots (N-CQDs) in terms of their biocompatibility and internalization by different cells. Surprisingly, N-CQD uptake does not contribute to the increased oxidative stress inside cells and lacks cytotoxic influence even at high concentrations, primarily through protein corona formation. We proved experimentally that the protein coating effectively limits the oxidative capacity of N-CQDs. Thus, N-CQDs served as an immobilization support for three different enzymes with the potential to be used as therapeutics. Various kinetic parameters of immobilized enzymes were analyzed. Regardless of the enzyme structure and type of reaction catalyzed, adsorption on the nanocarrier resulted in increased catalytic efficiency. The enzymatic-protein-to-nanomaterial ratio is the pivotal factor determining the course of kinetic parameter changes that can be tailored for enzyme application. We conclude that the above properties of N-CQDs make them an ideal support for enzymatic drugs required for multiple biomedical applications, including personalized medical therapies. MDPI 2021-07-29 /pmc/articles/PMC8347256/ /pubmed/34360901 http://dx.doi.org/10.3390/ijms22158136 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Czarnecka, Joanna Kwiatkowski, Mateusz Wiśniewski, Marek Roszek, Katarzyna Protein Corona Hinders N-CQDs Oxidative Potential and Favors Their Application as Nanobiocatalytic System |
title | Protein Corona Hinders N-CQDs Oxidative Potential and Favors Their Application as Nanobiocatalytic System |
title_full | Protein Corona Hinders N-CQDs Oxidative Potential and Favors Their Application as Nanobiocatalytic System |
title_fullStr | Protein Corona Hinders N-CQDs Oxidative Potential and Favors Their Application as Nanobiocatalytic System |
title_full_unstemmed | Protein Corona Hinders N-CQDs Oxidative Potential and Favors Their Application as Nanobiocatalytic System |
title_short | Protein Corona Hinders N-CQDs Oxidative Potential and Favors Their Application as Nanobiocatalytic System |
title_sort | protein corona hinders n-cqds oxidative potential and favors their application as nanobiocatalytic system |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8347256/ https://www.ncbi.nlm.nih.gov/pubmed/34360901 http://dx.doi.org/10.3390/ijms22158136 |
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