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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...

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Autores principales: Kilper, Stefan, Jahnke, Timotheus, Wiegers, Katharina, Grohe, Vera, Burghard, Zaklina, Bill, Joachim, Rothenstein, Dirk
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
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.
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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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