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Updated: Jan 26, 2026

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
Published on: January 26, 2024
Domain Diversity and Polarization Switching in Amino Acid β-Glycine
Daria Vasileva1, Semen Vasilev2,3, Andrei L Kholkin4,5
1School of Natural Sciences and Mathematics, Ural Federal University, Ekaterinburg 620000, Russia. daria.vasileva@urfu.ru.
Abstract:
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.
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