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Fate of the capping agent of biologically produced gold nanoparticles and adsorption of enzymes onto their surface

Enzymotherapy based on DNase I or RNase A has often been suggested as an optional strategy for cancer treatment. The efficacy of such procedures is limited e.g. by a short half-time of the enzymes or a low rate of their internalization. The use of nanoparticles, such as gold nanoparticles (AuNPs), h...

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Autores principales: Pourali, Parastoo, Dzmitruk, Volha, Pátek, Miroslav, Neuhöferová, Eva, Svoboda, Milan, Benson, Veronika
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10039949/
https://www.ncbi.nlm.nih.gov/pubmed/36966192
http://dx.doi.org/10.1038/s41598-023-31792-5
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author Pourali, Parastoo
Dzmitruk, Volha
Pátek, Miroslav
Neuhöferová, Eva
Svoboda, Milan
Benson, Veronika
author_facet Pourali, Parastoo
Dzmitruk, Volha
Pátek, Miroslav
Neuhöferová, Eva
Svoboda, Milan
Benson, Veronika
author_sort Pourali, Parastoo
collection PubMed
description Enzymotherapy based on DNase I or RNase A has often been suggested as an optional strategy for cancer treatment. The efficacy of such procedures is limited e.g. by a short half-time of the enzymes or a low rate of their internalization. The use of nanoparticles, such as gold nanoparticles (AuNPs), helps to overcome these limits. Specifically, biologically produced AuNPs represent an interesting variant here due to naturally occurring capping agents (CA) on their surface. The composition of the CA depends on the producing microorganism. CAs are responsible for the stabilization of the nanoparticles, and promote the direct linking of targeting and therapeutic molecules. This study provided proof of enzyme adsorption onto gold nanoparticles and digestion efficacy of AuNPs-adsorbed enzymes. We employed Fusarium oxysporum extract to produce AuNPs. These nanoparticles were round or polygonal with a size of about 5 nm, negative surface charge of about − 33 mV, and maximum absorption peak at 530 nm. After the adsorption of DNAse I, RNase A, or Proteinase K onto the AuNPs surface, the nanoparticles exhibited shifts in surface charge (values between − 22 and − 13 mV) and maximum absorption peak (values between 513 and 534 nm). The ability of AuNP-enzyme complexes to digest different targets was compared to enzymes alone. We found a remarkable degradation of ssDNA, and dsDNA by AuNP-DNAse I, and a modest degradation of ssRNA by AuNP-RNase A. The presence of particular enzymes on the AuNP surface was proved by liquid chromatography–mass spectrometry (LC–MS). Using SDS-PAGE electrophoresis, we detected a remarkable digestion of collagen type I and fibrinogen by AuNP-proteinase K complexes. We concluded that the biologically produced AuNPs directly bound DNase I, RNase A, and proteinase K while preserving their ability to digest specific targets. Therefore, according to our results, AuNPs can be used as effective enzyme carriers and the AuNP-enzyme conjugates can be effective tools for enzymotherapy.
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spelling pubmed-100399492023-03-27 Fate of the capping agent of biologically produced gold nanoparticles and adsorption of enzymes onto their surface Pourali, Parastoo Dzmitruk, Volha Pátek, Miroslav Neuhöferová, Eva Svoboda, Milan Benson, Veronika Sci Rep Article Enzymotherapy based on DNase I or RNase A has often been suggested as an optional strategy for cancer treatment. The efficacy of such procedures is limited e.g. by a short half-time of the enzymes or a low rate of their internalization. The use of nanoparticles, such as gold nanoparticles (AuNPs), helps to overcome these limits. Specifically, biologically produced AuNPs represent an interesting variant here due to naturally occurring capping agents (CA) on their surface. The composition of the CA depends on the producing microorganism. CAs are responsible for the stabilization of the nanoparticles, and promote the direct linking of targeting and therapeutic molecules. This study provided proof of enzyme adsorption onto gold nanoparticles and digestion efficacy of AuNPs-adsorbed enzymes. We employed Fusarium oxysporum extract to produce AuNPs. These nanoparticles were round or polygonal with a size of about 5 nm, negative surface charge of about − 33 mV, and maximum absorption peak at 530 nm. After the adsorption of DNAse I, RNase A, or Proteinase K onto the AuNPs surface, the nanoparticles exhibited shifts in surface charge (values between − 22 and − 13 mV) and maximum absorption peak (values between 513 and 534 nm). The ability of AuNP-enzyme complexes to digest different targets was compared to enzymes alone. We found a remarkable degradation of ssDNA, and dsDNA by AuNP-DNAse I, and a modest degradation of ssRNA by AuNP-RNase A. The presence of particular enzymes on the AuNP surface was proved by liquid chromatography–mass spectrometry (LC–MS). Using SDS-PAGE electrophoresis, we detected a remarkable digestion of collagen type I and fibrinogen by AuNP-proteinase K complexes. We concluded that the biologically produced AuNPs directly bound DNase I, RNase A, and proteinase K while preserving their ability to digest specific targets. Therefore, according to our results, AuNPs can be used as effective enzyme carriers and the AuNP-enzyme conjugates can be effective tools for enzymotherapy. Nature Publishing Group UK 2023-03-25 /pmc/articles/PMC10039949/ /pubmed/36966192 http://dx.doi.org/10.1038/s41598-023-31792-5 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Pourali, Parastoo
Dzmitruk, Volha
Pátek, Miroslav
Neuhöferová, Eva
Svoboda, Milan
Benson, Veronika
Fate of the capping agent of biologically produced gold nanoparticles and adsorption of enzymes onto their surface
title Fate of the capping agent of biologically produced gold nanoparticles and adsorption of enzymes onto their surface
title_full Fate of the capping agent of biologically produced gold nanoparticles and adsorption of enzymes onto their surface
title_fullStr Fate of the capping agent of biologically produced gold nanoparticles and adsorption of enzymes onto their surface
title_full_unstemmed Fate of the capping agent of biologically produced gold nanoparticles and adsorption of enzymes onto their surface
title_short Fate of the capping agent of biologically produced gold nanoparticles and adsorption of enzymes onto their surface
title_sort fate of the capping agent of biologically produced gold nanoparticles and adsorption of enzymes onto their surface
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10039949/
https://www.ncbi.nlm.nih.gov/pubmed/36966192
http://dx.doi.org/10.1038/s41598-023-31792-5
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