Tip-induced domain structures and polarization switching in ferroelectric amino acid glycine
- CICECO-Aveiro Institute of Materials and Department of Physics, University of Aveiro, 3810-193 Aveiro (Portugal)
- TEMA and Department of Mechanical Engineering, University of Aveiro, 3810-193 Aveiro (Portugal)
- Institute of Natural Sciences, Ural Federal University, 620000 Ekaterinburg (Russian Federation)
- Moscow State Institute of Radioengineering, Electronics and Automation, 119454 Moscow (Russian Federation)
- Conway Institute of Biomolecular and Biomedical Research and School of Physics, University College Dublin, Dublin (Ireland)
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 β-glycine, representing a broad class of non-centrosymmetric amino acids. We show that β-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 β-glycine are controlled by the charged domain walls which in turn can be manipulated by an external bias.
- OSTI ID:
- 22494747
- Journal Information:
- Journal of Applied Physics, Vol. 118, Issue 7; Other Information: (c) 2015 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA); ISSN 0021-8979
- Country of Publication:
- United States
- Language:
- English
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