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Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function
Gold nanoparticles provide a user-friendly and efficient surface for immobilization of enzymes and proteins. In this paper, we present a novel approach for enzyme bioconjugation to gold nanostars (AuNSs). AuNSs were modified with l-cysteine (Cys) and covalently bound to N-hydroxysulfosuccinimide (su...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6549951/ https://www.ncbi.nlm.nih.gov/pubmed/31218060 http://dx.doi.org/10.1098/rsos.190205 |
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author | Moses Phiri, Masauso Wingrove Mulder, Danielle Mason, Shayne Christiaan Vorster, Barend |
author_facet | Moses Phiri, Masauso Wingrove Mulder, Danielle Mason, Shayne Christiaan Vorster, Barend |
author_sort | Moses Phiri, Masauso |
collection | PubMed |
description | Gold nanoparticles provide a user-friendly and efficient surface for immobilization of enzymes and proteins. In this paper, we present a novel approach for enzyme bioconjugation to gold nanostars (AuNSs). AuNSs were modified with l-cysteine (Cys) and covalently bound to N-hydroxysulfosuccinimide (sulfo-NHS) activated intermediate glucose oxidase (GOx) to fabricate a stable and sensitive AuNSs–Cys–GOx bioconjugate complex. Such a strategy has the potential for increased attachment affinity without protein adsorption onto the AuNSs surface. Good dispersity in buffer suspension was observed, as well as stability in high ionic environments. Using the AuNSs–Cys–GOx bioconjugates showed greater sensitivity in the measuring of low concentrations of glucose based on plasmonic and colorimetric detection. Such a novel approach for enzyme immobilization can lead to AuNSs–Cys–GOx bioconjugate complexes that can be used as catalytic nanodevices in nanobiosensors based on oxidases in biomedical applications. |
format | Online Article Text |
id | pubmed-6549951 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-65499512019-06-19 Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function Moses Phiri, Masauso Wingrove Mulder, Danielle Mason, Shayne Christiaan Vorster, Barend R Soc Open Sci Chemistry Gold nanoparticles provide a user-friendly and efficient surface for immobilization of enzymes and proteins. In this paper, we present a novel approach for enzyme bioconjugation to gold nanostars (AuNSs). AuNSs were modified with l-cysteine (Cys) and covalently bound to N-hydroxysulfosuccinimide (sulfo-NHS) activated intermediate glucose oxidase (GOx) to fabricate a stable and sensitive AuNSs–Cys–GOx bioconjugate complex. Such a strategy has the potential for increased attachment affinity without protein adsorption onto the AuNSs surface. Good dispersity in buffer suspension was observed, as well as stability in high ionic environments. Using the AuNSs–Cys–GOx bioconjugates showed greater sensitivity in the measuring of low concentrations of glucose based on plasmonic and colorimetric detection. Such a novel approach for enzyme immobilization can lead to AuNSs–Cys–GOx bioconjugate complexes that can be used as catalytic nanodevices in nanobiosensors based on oxidases in biomedical applications. The Royal Society 2019-05-01 /pmc/articles/PMC6549951/ /pubmed/31218060 http://dx.doi.org/10.1098/rsos.190205 Text en © 2019 The Authors. http://creativecommons.org/licenses/by/4.0/ Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Chemistry Moses Phiri, Masauso Wingrove Mulder, Danielle Mason, Shayne Christiaan Vorster, Barend Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function |
title | Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function |
title_full | Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function |
title_fullStr | Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function |
title_full_unstemmed | Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function |
title_short | Facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function |
title_sort | facile immobilization of glucose oxidase onto gold nanostars with enhanced binding affinity and optimal function |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6549951/ https://www.ncbi.nlm.nih.gov/pubmed/31218060 http://dx.doi.org/10.1098/rsos.190205 |
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