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Quantification of Peptide-Bound Particles: A Phage Mimicking Approach via Site-Selective Immobilization on Glass
[Image: see text] The increasing complexity and need of high-tech materials for modern electronics raise the demand for rare earth elements. While recycling rates are still negligible for most elements, geopolitical tensions, circular economy, and the aim for a carbon-neutral society put pressure on...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8756571/ https://www.ncbi.nlm.nih.gov/pubmed/35036690 http://dx.doi.org/10.1021/acsomega.1c04343 |
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author | Schrader, Martin Bobeth, Caroline Lederer, Franziska L. |
author_facet | Schrader, Martin Bobeth, Caroline Lederer, Franziska L. |
author_sort | Schrader, Martin |
collection | PubMed |
description | [Image: see text] The increasing complexity and need of high-tech materials for modern electronics raise the demand for rare earth elements. While recycling rates are still negligible for most elements, geopolitical tensions, circular economy, and the aim for a carbon-neutral society put pressure on conventional supply strategies and emphasize the need for new ideas for recycling. Our research group works on the development of phage surface display (PSD)-derived peptide-based recycling methods for electronic waste. This study focuses on LaPO(4):Ce,Tb (LAP), a component of electronic waste from compact energy-saving lamps containing rare earth element-enriched fluorescent powders. While free solution-phase peptides show little to no interaction with the target material, we re-enabled the binding capability by immobilizing them on various glass supports. We shine a spotlight on the transition from phage-bound to free peptides and present the first proof of successful peptide-LAP particle interactions of previously reported PSD-derived sequences. Therefore, we introduce a method to investigate peptide–particle–interactions qualitatively and quantitatively. Additionally, a calibration curve allowed the quantification of peptide-bound particles. Combined with the quantification of the immobilized peptide on the surface, it was possible to calculate a potential dosage of peptides for future recycling processes. |
format | Online Article Text |
id | pubmed-8756571 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-87565712022-01-13 Quantification of Peptide-Bound Particles: A Phage Mimicking Approach via Site-Selective Immobilization on Glass Schrader, Martin Bobeth, Caroline Lederer, Franziska L. ACS Omega [Image: see text] The increasing complexity and need of high-tech materials for modern electronics raise the demand for rare earth elements. While recycling rates are still negligible for most elements, geopolitical tensions, circular economy, and the aim for a carbon-neutral society put pressure on conventional supply strategies and emphasize the need for new ideas for recycling. Our research group works on the development of phage surface display (PSD)-derived peptide-based recycling methods for electronic waste. This study focuses on LaPO(4):Ce,Tb (LAP), a component of electronic waste from compact energy-saving lamps containing rare earth element-enriched fluorescent powders. While free solution-phase peptides show little to no interaction with the target material, we re-enabled the binding capability by immobilizing them on various glass supports. We shine a spotlight on the transition from phage-bound to free peptides and present the first proof of successful peptide-LAP particle interactions of previously reported PSD-derived sequences. Therefore, we introduce a method to investigate peptide–particle–interactions qualitatively and quantitatively. Additionally, a calibration curve allowed the quantification of peptide-bound particles. Combined with the quantification of the immobilized peptide on the surface, it was possible to calculate a potential dosage of peptides for future recycling processes. American Chemical Society 2021-12-20 /pmc/articles/PMC8756571/ /pubmed/35036690 http://dx.doi.org/10.1021/acsomega.1c04343 Text en © 2021 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 | Schrader, Martin Bobeth, Caroline Lederer, Franziska L. Quantification of Peptide-Bound Particles: A Phage Mimicking Approach via Site-Selective Immobilization on Glass |
title | Quantification of Peptide-Bound Particles: A Phage
Mimicking Approach via Site-Selective Immobilization on Glass |
title_full | Quantification of Peptide-Bound Particles: A Phage
Mimicking Approach via Site-Selective Immobilization on Glass |
title_fullStr | Quantification of Peptide-Bound Particles: A Phage
Mimicking Approach via Site-Selective Immobilization on Glass |
title_full_unstemmed | Quantification of Peptide-Bound Particles: A Phage
Mimicking Approach via Site-Selective Immobilization on Glass |
title_short | Quantification of Peptide-Bound Particles: A Phage
Mimicking Approach via Site-Selective Immobilization on Glass |
title_sort | quantification of peptide-bound particles: a phage
mimicking approach via site-selective immobilization on glass |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8756571/ https://www.ncbi.nlm.nih.gov/pubmed/35036690 http://dx.doi.org/10.1021/acsomega.1c04343 |
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