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Domain Diversity and Polarization Switching in Amino Acid β-Glycine
Piezoelectric materials based on lead zirconate titanate are widely used in sensors and actuators. However, their application is limited because of high processing temperature, brittleness, lack of conformal deposition and, more importantly, intrinsic incompatibility with biological environments. Re...
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/PMC6514944/ https://www.ncbi.nlm.nih.gov/pubmed/30991625 http://dx.doi.org/10.3390/ma12081223 |
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author | Vasileva, Daria Vasilev, Semen Kholkin, Andrei L. Shur, Vladimir Ya. |
author_facet | Vasileva, Daria Vasilev, Semen Kholkin, Andrei L. Shur, Vladimir Ya. |
author_sort | Vasileva, Daria |
collection | PubMed |
description | Piezoelectric materials based on lead zirconate titanate are widely used in sensors and actuators. However, their application is limited because of high processing temperature, brittleness, lack of conformal deposition and, more importantly, intrinsic incompatibility with biological environments. Recent studies on bioorganic piezoelectrics have demonstrated their potential in these applications, essentially due to using the same building blocks as those used by nature. In this work, we used piezoresponse force microscopy (PFM) to study the domain structures and polarization reversal in the smallest amino acid glycine, which recently attracted a lot of attention due to its strong shear piezoelectric activity. In this uniaxial ferroelectric, a diverse domain structure that includes both 180° and charged domain walls was observed, as well as domain wall kinks related to peculiar growth and crystallographic structure of this material. Local polarization switching was studied by applying a bias voltage to the PFM tip, and the possibility to control the resulting domain structure was demonstrated. This study has shown that the as-grown domain structure and changes in the electric field in glycine are qualitatively similar to those found in the uniaxial inorganic ferroelectrics. |
format | Online Article Text |
id | pubmed-6514944 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-65149442019-05-31 Domain Diversity and Polarization Switching in Amino Acid β-Glycine Vasileva, Daria Vasilev, Semen Kholkin, Andrei L. Shur, Vladimir Ya. Materials (Basel) Article Piezoelectric materials based on lead zirconate titanate are widely used in sensors and actuators. However, their application is limited because of high processing temperature, brittleness, lack of conformal deposition and, more importantly, intrinsic incompatibility with biological environments. Recent studies on bioorganic piezoelectrics have demonstrated their potential in these applications, essentially due to using the same building blocks as those used by nature. In this work, we used piezoresponse force microscopy (PFM) to study the domain structures and polarization reversal in the smallest amino acid glycine, which recently attracted a lot of attention due to its strong shear piezoelectric activity. In this uniaxial ferroelectric, a diverse domain structure that includes both 180° and charged domain walls was observed, as well as domain wall kinks related to peculiar growth and crystallographic structure of this material. Local polarization switching was studied by applying a bias voltage to the PFM tip, and the possibility to control the resulting domain structure was demonstrated. This study has shown that the as-grown domain structure and changes in the electric field in glycine are qualitatively similar to those found in the uniaxial inorganic ferroelectrics. MDPI 2019-04-15 /pmc/articles/PMC6514944/ /pubmed/30991625 http://dx.doi.org/10.3390/ma12081223 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 Vasileva, Daria Vasilev, Semen Kholkin, Andrei L. Shur, Vladimir Ya. Domain Diversity and Polarization Switching in Amino Acid β-Glycine |
title | Domain Diversity and Polarization Switching in Amino Acid β-Glycine |
title_full | Domain Diversity and Polarization Switching in Amino Acid β-Glycine |
title_fullStr | Domain Diversity and Polarization Switching in Amino Acid β-Glycine |
title_full_unstemmed | Domain Diversity and Polarization Switching in Amino Acid β-Glycine |
title_short | Domain Diversity and Polarization Switching in Amino Acid β-Glycine |
title_sort | domain diversity and polarization switching in amino acid β-glycine |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6514944/ https://www.ncbi.nlm.nih.gov/pubmed/30991625 http://dx.doi.org/10.3390/ma12081223 |
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