Tip-induced domain structures and polarization switching in ferroelectric amino acid glycine
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10773/20690 |
Resumo: | Bioorganic ferroelectrics and piezoelectrics are becoming increasingly important in view of their intrinsic compatibility with biological environment and biofunctionality combined with strong piezoelectric effect and a switchable polarization at room temperature. Here, we study tip-induced domain structures and polarization switching in the smallest amino acid beta-glycine, representing a broad class of non-centrosymmetric amino acids. We show that beta-glycine is indeed a room-temperature ferroelectric and polarization can be switched by applying a bias to non-polar cuts via a conducting tip of atomic force microscope (AFM). Dynamics of these in-plane domains is studied as a function of an applied voltage and pulse duration. The domain shape is dictated by polarization screening at the domain boundaries and mediated by growth defects. Thermodynamic theory is applied to explain the domain propagation induced by the AFM tip. Our findings suggest that the properties of beta-glycine are controlled by the charged domain walls which in turn can be manipulated by an external bias. (C) 2015 AIP Publishing LLC. |
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Tip-induced domain structures and polarization switching in ferroelectric amino acid glycineROOM-TEMPERATURE FERROELECTRICITYPHASE-TRANSFORMATIONFORCE MICROSCOPYNANOSCALECRYSTALSBioorganic ferroelectrics and piezoelectrics are becoming increasingly important in view of their intrinsic compatibility with biological environment and biofunctionality combined with strong piezoelectric effect and a switchable polarization at room temperature. Here, we study tip-induced domain structures and polarization switching in the smallest amino acid beta-glycine, representing a broad class of non-centrosymmetric amino acids. We show that beta-glycine is indeed a room-temperature ferroelectric and polarization can be switched by applying a bias to non-polar cuts via a conducting tip of atomic force microscope (AFM). Dynamics of these in-plane domains is studied as a function of an applied voltage and pulse duration. The domain shape is dictated by polarization screening at the domain boundaries and mediated by growth defects. Thermodynamic theory is applied to explain the domain propagation induced by the AFM tip. Our findings suggest that the properties of beta-glycine are controlled by the charged domain walls which in turn can be manipulated by an external bias. (C) 2015 AIP Publishing LLC.AMER INST PHYSICS2017-12-07T19:55:59Z2015-01-01T00:00:00Z2015info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/20690eng0021-897910.1063/1.4927807Seyedhosseini, E.Bdikin, I.Ivanov, M.Vasileva, D.Kudryavtsev, A.Rodriguez, B. J.Kholkin, A. L.info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-02-22T11:40:42Zoai:ria.ua.pt:10773/20690Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T02:55:21.286822Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Tip-induced domain structures and polarization switching in ferroelectric amino acid glycine |
title |
Tip-induced domain structures and polarization switching in ferroelectric amino acid glycine |
spellingShingle |
Tip-induced domain structures and polarization switching in ferroelectric amino acid glycine Seyedhosseini, E. ROOM-TEMPERATURE FERROELECTRICITY PHASE-TRANSFORMATION FORCE MICROSCOPY NANOSCALE CRYSTALS |
title_short |
Tip-induced domain structures and polarization switching in ferroelectric amino acid glycine |
title_full |
Tip-induced domain structures and polarization switching in ferroelectric amino acid glycine |
title_fullStr |
Tip-induced domain structures and polarization switching in ferroelectric amino acid glycine |
title_full_unstemmed |
Tip-induced domain structures and polarization switching in ferroelectric amino acid glycine |
title_sort |
Tip-induced domain structures and polarization switching in ferroelectric amino acid glycine |
author |
Seyedhosseini, E. |
author_facet |
Seyedhosseini, E. Bdikin, I. Ivanov, M. Vasileva, D. Kudryavtsev, A. Rodriguez, B. J. Kholkin, A. L. |
author_role |
author |
author2 |
Bdikin, I. Ivanov, M. Vasileva, D. Kudryavtsev, A. Rodriguez, B. J. Kholkin, A. L. |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Seyedhosseini, E. Bdikin, I. Ivanov, M. Vasileva, D. Kudryavtsev, A. Rodriguez, B. J. Kholkin, A. L. |
dc.subject.por.fl_str_mv |
ROOM-TEMPERATURE FERROELECTRICITY PHASE-TRANSFORMATION FORCE MICROSCOPY NANOSCALE CRYSTALS |
topic |
ROOM-TEMPERATURE FERROELECTRICITY PHASE-TRANSFORMATION FORCE MICROSCOPY NANOSCALE CRYSTALS |
description |
Bioorganic ferroelectrics and piezoelectrics are becoming increasingly important in view of their intrinsic compatibility with biological environment and biofunctionality combined with strong piezoelectric effect and a switchable polarization at room temperature. Here, we study tip-induced domain structures and polarization switching in the smallest amino acid beta-glycine, representing a broad class of non-centrosymmetric amino acids. We show that beta-glycine is indeed a room-temperature ferroelectric and polarization can be switched by applying a bias to non-polar cuts via a conducting tip of atomic force microscope (AFM). Dynamics of these in-plane domains is studied as a function of an applied voltage and pulse duration. The domain shape is dictated by polarization screening at the domain boundaries and mediated by growth defects. Thermodynamic theory is applied to explain the domain propagation induced by the AFM tip. Our findings suggest that the properties of beta-glycine are controlled by the charged domain walls which in turn can be manipulated by an external bias. (C) 2015 AIP Publishing LLC. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-01-01T00:00:00Z 2015 2017-12-07T19:55:59Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10773/20690 |
url |
http://hdl.handle.net/10773/20690 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0021-8979 10.1063/1.4927807 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
AMER INST PHYSICS |
publisher.none.fl_str_mv |
AMER INST PHYSICS |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799137606715310080 |