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Proteins enriched in charged amino acids control the formation and stabilization of selenium nanoparticles in Comamonas testosteroni S44
Elemental selenium nanoparticles (SeNPs) are useful in medicine, environmental remediation and in material science. Biosynthesized SeNPs (BioSeNPs) by bacteria are cheap, eco-friendly and have a lower cytotoxicity in comparison with chemically synthesized ones. Organic matters were found to cap on t...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5859168/ https://www.ncbi.nlm.nih.gov/pubmed/29555951 http://dx.doi.org/10.1038/s41598-018-23295-5 |
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author | Xu, Ding Yang, Lichen Wang, Yu Wang, Gejiao Rensing, Christopher Zheng, Shixue |
author_facet | Xu, Ding Yang, Lichen Wang, Yu Wang, Gejiao Rensing, Christopher Zheng, Shixue |
author_sort | Xu, Ding |
collection | PubMed |
description | Elemental selenium nanoparticles (SeNPs) are useful in medicine, environmental remediation and in material science. Biosynthesized SeNPs (BioSeNPs) by bacteria are cheap, eco-friendly and have a lower cytotoxicity in comparison with chemically synthesized ones. Organic matters were found to cap on the surface of BioSeNPs, but the functions were still not entirely clear. The purified BioSeNPs were coated in a thick layer of organic substrates observed by transmission electron microscopy (TEM). Fourier Transform Infrared (FT-IR) and quantitative detection of the coating agents showed that one gram of purified BioSeNPs bound 1069 mg proteins, 23 mg carbohydrates and only very limited amounts of lipids. Proteomics of BioSeNPs showed more than 800 proteins bound to BioSeNPs. Proteins enriched in charged amino acids are the major factor thought to govern the formation process and stabilization of BioSeNPs in bacteria. In view of the results reported here, a schematic model for the molecular mechanism of BioSeNPs formation in bacteria is proposed. These findings are helpful for the artificial green synthesis of stable SeNPs under specific condition and guiding the surface modification of SeNPs for medicine application. |
format | Online Article Text |
id | pubmed-5859168 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-58591682018-03-20 Proteins enriched in charged amino acids control the formation and stabilization of selenium nanoparticles in Comamonas testosteroni S44 Xu, Ding Yang, Lichen Wang, Yu Wang, Gejiao Rensing, Christopher Zheng, Shixue Sci Rep Article Elemental selenium nanoparticles (SeNPs) are useful in medicine, environmental remediation and in material science. Biosynthesized SeNPs (BioSeNPs) by bacteria are cheap, eco-friendly and have a lower cytotoxicity in comparison with chemically synthesized ones. Organic matters were found to cap on the surface of BioSeNPs, but the functions were still not entirely clear. The purified BioSeNPs were coated in a thick layer of organic substrates observed by transmission electron microscopy (TEM). Fourier Transform Infrared (FT-IR) and quantitative detection of the coating agents showed that one gram of purified BioSeNPs bound 1069 mg proteins, 23 mg carbohydrates and only very limited amounts of lipids. Proteomics of BioSeNPs showed more than 800 proteins bound to BioSeNPs. Proteins enriched in charged amino acids are the major factor thought to govern the formation process and stabilization of BioSeNPs in bacteria. In view of the results reported here, a schematic model for the molecular mechanism of BioSeNPs formation in bacteria is proposed. These findings are helpful for the artificial green synthesis of stable SeNPs under specific condition and guiding the surface modification of SeNPs for medicine application. Nature Publishing Group UK 2018-03-19 /pmc/articles/PMC5859168/ /pubmed/29555951 http://dx.doi.org/10.1038/s41598-018-23295-5 Text en © The Author(s) 2018 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Xu, Ding Yang, Lichen Wang, Yu Wang, Gejiao Rensing, Christopher Zheng, Shixue Proteins enriched in charged amino acids control the formation and stabilization of selenium nanoparticles in Comamonas testosteroni S44 |
title | Proteins enriched in charged amino acids control the formation and stabilization of selenium nanoparticles in Comamonas testosteroni S44 |
title_full | Proteins enriched in charged amino acids control the formation and stabilization of selenium nanoparticles in Comamonas testosteroni S44 |
title_fullStr | Proteins enriched in charged amino acids control the formation and stabilization of selenium nanoparticles in Comamonas testosteroni S44 |
title_full_unstemmed | Proteins enriched in charged amino acids control the formation and stabilization of selenium nanoparticles in Comamonas testosteroni S44 |
title_short | Proteins enriched in charged amino acids control the formation and stabilization of selenium nanoparticles in Comamonas testosteroni S44 |
title_sort | proteins enriched in charged amino acids control the formation and stabilization of selenium nanoparticles in comamonas testosteroni s44 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5859168/ https://www.ncbi.nlm.nih.gov/pubmed/29555951 http://dx.doi.org/10.1038/s41598-018-23295-5 |
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