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| Home > Publications database > Electric‑field induced modulation of amorphous protein-salt aggregates and phase behavior |
| Poster (Other) | FZJ-2023-05706 |
2023
Abstract: Proteins in their native state are marginally stable and tend to aggregate. Controlling protein aggregation is very important, but still a major challenge in various fields, including medicine, pharmacology, food processing, and materials science. The flexible, amorphous, micron-sized protein aggregates composed of lysozyme molecules reduced by dithiothreitol are used for a model system that are exposed to a weak alternating current electric field. Their field response is followed an in situ by time-resolved polarized optical microscopy, revealing field-induced deformation, reorientation and enhanced polarization as well as the disintegration of large clusters of aggregates [1]. Also, the lysozyme crystal in salt solutions are investigated by the phase diagram in the presence of electric fields [2], underlying the gas-liquid and liquid-liquid phase separation in the early stage of protein aggregates. In addition, the effects of fatty acid, ionic strength, and the weak AC electric field in basic functional protein BSA solutions [3], are explored by the collective microscopic dynamics of interacting protein aggregates. These protein aggregates in the phase behavior are then fundamentally interesting in the driving formation of microscopic elongation of anisotropic growth. [1] Kyongok Kang and Florian Platten, “Electric‑field induced modulation of amorphous protein aggregates: polarization, deformation, and reorientation”, Scientific Reports 12:3061 (2022).[2] D. Ray, K. Kang, and F. Platten et al, “Lysozyme-salt protein aggregates in electric-fields”, in preparation (2023).[3] Kyongok Kang, “The effect of fatty acids, ionic strength, and electric fields on the microscopic dynamics of BSA aggregates, Frontiers in Physics 11:1282099 (2023)
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