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Biomining of MoS(2) with Peptide-based Smart Biomaterials
Biomining of valuable metals using a target specific approach promises increased purification yields and decreased cost. Target specificity can be implemented with proteins/peptides, the biological molecules, responsible from various structural and functional pathways in living organisms by virtue o...
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/PMC5820330/ https://www.ncbi.nlm.nih.gov/pubmed/29463859 http://dx.doi.org/10.1038/s41598-018-21692-4 |
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author | Cetinel, Sibel Shen, Wei-Zheng Aminpour, Maral Bhomkar, Prasanna Wang, Feng Borujeny, Elham Rafie Sharma, Kumakshi Nayebi, Niloofar Montemagno, Carlo |
author_facet | Cetinel, Sibel Shen, Wei-Zheng Aminpour, Maral Bhomkar, Prasanna Wang, Feng Borujeny, Elham Rafie Sharma, Kumakshi Nayebi, Niloofar Montemagno, Carlo |
author_sort | Cetinel, Sibel |
collection | PubMed |
description | Biomining of valuable metals using a target specific approach promises increased purification yields and decreased cost. Target specificity can be implemented with proteins/peptides, the biological molecules, responsible from various structural and functional pathways in living organisms by virtue of their specific recognition abilities towards both organic and inorganic materials. Phage display libraries are used to identify peptide biomolecules capable of specifically recognizing and binding organic/inorganic materials of interest with high affinities. Using combinatorial approaches, these molecular recognition elements can be converted into smart hybrid biomaterials and harnessed for biotechnological applications. Herein, we used a commercially available phage-display library to identify peptides with specific binding affinity to molybdenite (MoS(2)) and used them to decorate magnetic NPs. These peptide-coupled NPs could capture MoS(2) under a variety of environmental conditions. The same batch of NPs could be re-used multiple times to harvest MoS(2), clearly suggesting that this hybrid material was robust and recyclable. The advantages of this smart hybrid biomaterial with respect to its MoS(2)-binding specificity, robust performance under environmentally challenging conditions and its recyclability suggests its potential application in harvesting MoS(2) from tailing ponds and downstream mining processes. |
format | Online Article Text |
id | pubmed-5820330 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-58203302018-02-26 Biomining of MoS(2) with Peptide-based Smart Biomaterials Cetinel, Sibel Shen, Wei-Zheng Aminpour, Maral Bhomkar, Prasanna Wang, Feng Borujeny, Elham Rafie Sharma, Kumakshi Nayebi, Niloofar Montemagno, Carlo Sci Rep Article Biomining of valuable metals using a target specific approach promises increased purification yields and decreased cost. Target specificity can be implemented with proteins/peptides, the biological molecules, responsible from various structural and functional pathways in living organisms by virtue of their specific recognition abilities towards both organic and inorganic materials. Phage display libraries are used to identify peptide biomolecules capable of specifically recognizing and binding organic/inorganic materials of interest with high affinities. Using combinatorial approaches, these molecular recognition elements can be converted into smart hybrid biomaterials and harnessed for biotechnological applications. Herein, we used a commercially available phage-display library to identify peptides with specific binding affinity to molybdenite (MoS(2)) and used them to decorate magnetic NPs. These peptide-coupled NPs could capture MoS(2) under a variety of environmental conditions. The same batch of NPs could be re-used multiple times to harvest MoS(2), clearly suggesting that this hybrid material was robust and recyclable. The advantages of this smart hybrid biomaterial with respect to its MoS(2)-binding specificity, robust performance under environmentally challenging conditions and its recyclability suggests its potential application in harvesting MoS(2) from tailing ponds and downstream mining processes. Nature Publishing Group UK 2018-02-20 /pmc/articles/PMC5820330/ /pubmed/29463859 http://dx.doi.org/10.1038/s41598-018-21692-4 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 Cetinel, Sibel Shen, Wei-Zheng Aminpour, Maral Bhomkar, Prasanna Wang, Feng Borujeny, Elham Rafie Sharma, Kumakshi Nayebi, Niloofar Montemagno, Carlo Biomining of MoS(2) with Peptide-based Smart Biomaterials |
title | Biomining of MoS(2) with Peptide-based Smart Biomaterials |
title_full | Biomining of MoS(2) with Peptide-based Smart Biomaterials |
title_fullStr | Biomining of MoS(2) with Peptide-based Smart Biomaterials |
title_full_unstemmed | Biomining of MoS(2) with Peptide-based Smart Biomaterials |
title_short | Biomining of MoS(2) with Peptide-based Smart Biomaterials |
title_sort | biomining of mos(2) with peptide-based smart biomaterials |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5820330/ https://www.ncbi.nlm.nih.gov/pubmed/29463859 http://dx.doi.org/10.1038/s41598-018-21692-4 |
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