Tip-induced domain structures and polarization switching in ferroelectric amino acid glycine

Detalhes bibliográficos
Autor(a) principal: Seyedhosseini, E.
Data de Publicação: 2015
Outros Autores: Bdikin, I., Ivanov, M., Vasileva, D., Kudryavtsev, A., Rodriguez, B. J., Kholkin, A. L.
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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spelling 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)
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instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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