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Peptide Controlled Shaping of Biomineralized Tin(II) Oxide into Flower-Like Particles
The size and morphology of metal oxide particles have a large impact on the physicochemical properties of these materials, e.g., the aspect ratio of particles affects their catalytic activity. Bioinspired synthesis routes give the opportunity to control precisely the structure and aspect ratio of th...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6470704/ https://www.ncbi.nlm.nih.gov/pubmed/30889924 http://dx.doi.org/10.3390/ma12060904 |
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author | Kilper, Stefan Jahnke, Timotheus Wiegers, Katharina Grohe, Vera Burghard, Zaklina Bill, Joachim Rothenstein, Dirk |
author_facet | Kilper, Stefan Jahnke, Timotheus Wiegers, Katharina Grohe, Vera Burghard, Zaklina Bill, Joachim Rothenstein, Dirk |
author_sort | Kilper, Stefan |
collection | PubMed |
description | The size and morphology of metal oxide particles have a large impact on the physicochemical properties of these materials, e.g., the aspect ratio of particles affects their catalytic activity. Bioinspired synthesis routes give the opportunity to control precisely the structure and aspect ratio of the metal oxide particles by bioorganic molecules, such as peptides. This study focusses on the identification of tin(II) oxide (tin monoxide, SnO) binding peptides, and their effect on the synthesis of crystalline SnO microstructures. The phage display technique was used to identify the 7-mer peptide SnBP01 (LPPWKLK), which shows a high binding affinity towards crystalline SnO. It was found that the derivatives of the SnBP01 peptide, varying in peptide length and thus in their interaction, significantly affect the aspect ratio and the size dimension of mineralized SnO particles, resulting in flower-like morphology. Furthermore, the important role of the N-terminal leucine residue in the peptide for the strong organic–inorganic interaction was revealed by FTIR investigations. This bioinspired approach shows a facile procedure for the detailed investigation of peptide-to-metal oxide interactions, as well as an easy method for the controlled synthesis of tin(II) oxide particles with different morphologies. |
format | Online Article Text |
id | pubmed-6470704 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-64707042019-04-27 Peptide Controlled Shaping of Biomineralized Tin(II) Oxide into Flower-Like Particles Kilper, Stefan Jahnke, Timotheus Wiegers, Katharina Grohe, Vera Burghard, Zaklina Bill, Joachim Rothenstein, Dirk Materials (Basel) Article The size and morphology of metal oxide particles have a large impact on the physicochemical properties of these materials, e.g., the aspect ratio of particles affects their catalytic activity. Bioinspired synthesis routes give the opportunity to control precisely the structure and aspect ratio of the metal oxide particles by bioorganic molecules, such as peptides. This study focusses on the identification of tin(II) oxide (tin monoxide, SnO) binding peptides, and their effect on the synthesis of crystalline SnO microstructures. The phage display technique was used to identify the 7-mer peptide SnBP01 (LPPWKLK), which shows a high binding affinity towards crystalline SnO. It was found that the derivatives of the SnBP01 peptide, varying in peptide length and thus in their interaction, significantly affect the aspect ratio and the size dimension of mineralized SnO particles, resulting in flower-like morphology. Furthermore, the important role of the N-terminal leucine residue in the peptide for the strong organic–inorganic interaction was revealed by FTIR investigations. This bioinspired approach shows a facile procedure for the detailed investigation of peptide-to-metal oxide interactions, as well as an easy method for the controlled synthesis of tin(II) oxide particles with different morphologies. MDPI 2019-03-18 /pmc/articles/PMC6470704/ /pubmed/30889924 http://dx.doi.org/10.3390/ma12060904 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Kilper, Stefan Jahnke, Timotheus Wiegers, Katharina Grohe, Vera Burghard, Zaklina Bill, Joachim Rothenstein, Dirk Peptide Controlled Shaping of Biomineralized Tin(II) Oxide into Flower-Like Particles |
title | Peptide Controlled Shaping of Biomineralized Tin(II) Oxide into Flower-Like Particles |
title_full | Peptide Controlled Shaping of Biomineralized Tin(II) Oxide into Flower-Like Particles |
title_fullStr | Peptide Controlled Shaping of Biomineralized Tin(II) Oxide into Flower-Like Particles |
title_full_unstemmed | Peptide Controlled Shaping of Biomineralized Tin(II) Oxide into Flower-Like Particles |
title_short | Peptide Controlled Shaping of Biomineralized Tin(II) Oxide into Flower-Like Particles |
title_sort | peptide controlled shaping of biomineralized tin(ii) oxide into flower-like particles |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6470704/ https://www.ncbi.nlm.nih.gov/pubmed/30889924 http://dx.doi.org/10.3390/ma12060904 |
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