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Bioreduction of Gold Ions under Greener Conditions by the Thiol-Modified M13 Bacteriophage and with Hydroxylamine as the Autocatalytic Reducing Agent
[Image: see text] Bioreduction of gold ions by the thiol-modified M13 bacteriophage (M13-SH) has been exploited as the potential alternative to conventional methods based on toxic chemicals, due to the gold affinity of the thiol groups, inherent gold reduction, and high specific surface area of the...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8945180/ https://www.ncbi.nlm.nih.gov/pubmed/35350307 http://dx.doi.org/10.1021/acsomega.2c00563 |
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author | Wei, Zongwu Wei, Xueyan Zhao, Chenxi Zhang, Han Zhang, Zhenkun |
author_facet | Wei, Zongwu Wei, Xueyan Zhao, Chenxi Zhang, Han Zhang, Zhenkun |
author_sort | Wei, Zongwu |
collection | PubMed |
description | [Image: see text] Bioreduction of gold ions by the thiol-modified M13 bacteriophage (M13-SH) has been exploited as the potential alternative to conventional methods based on toxic chemicals, due to the gold affinity of the thiol groups, inherent gold reduction, and high specific surface area of the filamentous virus. Such efforts have been hindered by harsh conditions involving strong reducing agents and extreme pH that are harmful to the virus. Herein, a virus-friendly and greener method of bioreduction of AuCl(4)(–) at neutral pH based on M13-SH is demonstrated. M13-SH was prepared by coupling the virus with N-succinimidyl S-acetylthioacetate, followed by deacylation in the presence of hydroxylamine·HCl to expose the thiol groups. The key finding is that without time-consuming purification, the mixture after deacylation consisting of M13-SH, residual hydroxylamine, and so forth can directly turn ionic gold species into gold, leading to macroscopic precipitated products with interconnected linear structures consisting of fused gold nanoparticles. Besides working as the virus-friendly reducing agent with a unique autocatalytic style, hydroxylamine diminishes disulfide bonding-induced intervirus bundling of M13-SH so as to maintain its efficient biosorption of ionic gold precursors. This work demonstrates a general and green strategy of bioreduction of gold via combination of the gold-affinity proteins or organisms and the unique autocatalytic reduction of hydroxylamine. |
format | Online Article Text |
id | pubmed-8945180 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-89451802022-03-28 Bioreduction of Gold Ions under Greener Conditions by the Thiol-Modified M13 Bacteriophage and with Hydroxylamine as the Autocatalytic Reducing Agent Wei, Zongwu Wei, Xueyan Zhao, Chenxi Zhang, Han Zhang, Zhenkun ACS Omega [Image: see text] Bioreduction of gold ions by the thiol-modified M13 bacteriophage (M13-SH) has been exploited as the potential alternative to conventional methods based on toxic chemicals, due to the gold affinity of the thiol groups, inherent gold reduction, and high specific surface area of the filamentous virus. Such efforts have been hindered by harsh conditions involving strong reducing agents and extreme pH that are harmful to the virus. Herein, a virus-friendly and greener method of bioreduction of AuCl(4)(–) at neutral pH based on M13-SH is demonstrated. M13-SH was prepared by coupling the virus with N-succinimidyl S-acetylthioacetate, followed by deacylation in the presence of hydroxylamine·HCl to expose the thiol groups. The key finding is that without time-consuming purification, the mixture after deacylation consisting of M13-SH, residual hydroxylamine, and so forth can directly turn ionic gold species into gold, leading to macroscopic precipitated products with interconnected linear structures consisting of fused gold nanoparticles. Besides working as the virus-friendly reducing agent with a unique autocatalytic style, hydroxylamine diminishes disulfide bonding-induced intervirus bundling of M13-SH so as to maintain its efficient biosorption of ionic gold precursors. This work demonstrates a general and green strategy of bioreduction of gold via combination of the gold-affinity proteins or organisms and the unique autocatalytic reduction of hydroxylamine. American Chemical Society 2022-03-08 /pmc/articles/PMC8945180/ /pubmed/35350307 http://dx.doi.org/10.1021/acsomega.2c00563 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Wei, Zongwu Wei, Xueyan Zhao, Chenxi Zhang, Han Zhang, Zhenkun Bioreduction of Gold Ions under Greener Conditions by the Thiol-Modified M13 Bacteriophage and with Hydroxylamine as the Autocatalytic Reducing Agent |
title | Bioreduction of Gold Ions under Greener Conditions
by the Thiol-Modified M13 Bacteriophage and with Hydroxylamine as
the Autocatalytic Reducing Agent |
title_full | Bioreduction of Gold Ions under Greener Conditions
by the Thiol-Modified M13 Bacteriophage and with Hydroxylamine as
the Autocatalytic Reducing Agent |
title_fullStr | Bioreduction of Gold Ions under Greener Conditions
by the Thiol-Modified M13 Bacteriophage and with Hydroxylamine as
the Autocatalytic Reducing Agent |
title_full_unstemmed | Bioreduction of Gold Ions under Greener Conditions
by the Thiol-Modified M13 Bacteriophage and with Hydroxylamine as
the Autocatalytic Reducing Agent |
title_short | Bioreduction of Gold Ions under Greener Conditions
by the Thiol-Modified M13 Bacteriophage and with Hydroxylamine as
the Autocatalytic Reducing Agent |
title_sort | bioreduction of gold ions under greener conditions
by the thiol-modified m13 bacteriophage and with hydroxylamine as
the autocatalytic reducing agent |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8945180/ https://www.ncbi.nlm.nih.gov/pubmed/35350307 http://dx.doi.org/10.1021/acsomega.2c00563 |
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