SoftComp partners from Forschungszentrum Jülich and Heinrich Heine University Düsseldorf have uncovered the profound effects of electric fields on protein phase behaviour and crystallization. Their research offers valuable insights into how external electric fields can alter the behaviour of proteins at the molecular level.
The study explores the impact of alternating current (AC) electric fields on protein crystallization and liquid-liquid phase separation (LLPS). Notably, the research found that under weak AC electric fields, protein crystallization can occur in a broader region of the phase diagram. Additionally, the nucleation induction times were reduced, and crystal growth rates were enhanced, while LLPS was suppressed.
The team attributes these changes to modifications in the protein-protein interaction potential. Electric fields can alter protein interactions by influencing their conformation and surface properties, leading to enhanced short-range attractions between proteins. This finding has important implications for various fields, including pharmaceuticals, food engineering, and materials science.
By using lysozyme as a model system and acetate buffer with sodium thiocyanate, the researchers were able to observe significant shifts in the phase boundaries due to the electric field. The liquid-crystal boundary shifted towards lower salt concentrations, promoting crystallization, while the LLPS boundary shifted to higher salt concentrations, indicating a reduction in overall protein attractions.
This study not only advances our understanding of protein phase behaviour under external electric fields but also opens up new possibilities for controlling protein crystallization and phase separation. The findings suggest that electric fields could be used to fine-tune protein interactions and potentially design novel protein-based materials. The full protein phase diagram and associated phase transition kinetics in the presence of well-defined electric fields remain to be systematically explored.
Read more:
Ray D. et al., J. Phys. Chem. Lett., 15, 8108 (2024)
SoftComp partner:
Forschungszentrum Jülich (IBI-4)
