Pulsed electric fields induce modulation of protein liquid–liquid phase separation

Wang, Mengying; Schubert, Robin; Lorenzen, Kristina; Cheng, Qing-Di; Exner, Christian; Brognaro, H.; Mudogo, Célestin Nzanzu; Betzel, Christian

doi:10.1039/d0sm01478h

Cited by 7 publications

(6 citation statements)

References 52 publications

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“…The rate of assembly (as inferred from the DLS count rate, which convolves both number density and size) also appears to increase with voltage. The physical mechanism and utility of this process differs completely from those of AC field-mediated concentration, liquid-liquid phase segregation and crystallization of macromolecules [34][35][36][37].…”

Section: Discussionmentioning

confidence: 99%

Voltage-calibrated, finely tunable protein assembly

Lin

Masquelier

Sabeh

et al. 2023

J. R. Soc. Interface.

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Neuronally triggered phosphorylation drives the calibrated and cyclable assembly of the reflectin signal transducing proteins, resulting in their fine tuning of colours reflected from specialized skin cells in squid for camouflage and communication. In close parallel to this physiological behaviour, we demonstrate for the first time that electrochemical reduction of reflectin A1, used as a surrogate for charge neutralization by phosphorylation, triggers voltage-calibrated, proportional and cyclable control of the size of the protein's assembly. Electrochemically triggered condensation, folding and assembly were simultaneously analysed using in situ dynamic light scattering, circular dichroism and UV absorbance spectroscopies. The correlation of assembly size with applied potential is probably linked to reflectin's mechanism of dynamic arrest, which is controlled by the extent of neuronally triggered charge neutralization and the corresponding fine tuning of colour in the biological system. This work opens a new perspective on electrically controlling and simultaneously observing reflectin assembly and, more broadly, provides access to manipulate, observe and electrokinetically control the formation of intermediates and conformational dynamics of macromolecular systems.

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Section: Discussionmentioning

confidence: 99%

Voltage-calibrated, finely tunable protein assembly

Lin

Masquelier

Sabeh

et al. 2023

J. R. Soc. Interface.

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“…Wang et al conducted a crystallization experiment of glucose isomerase, ovalbumin, and bovine pancreatic trypsin inhibitor under the pulsed electric field. 92 With the assistance of transmission electron microscopy (TEM), and complementary polarized and depolarized dynamic light scattering (DLS/DDLS), it was observed that pulsed electric field could have effects on the morphology and spatial distributions of the protein liquid dense clusters, which were believed to be precursors of protein crystal nuclei. The effect of direct current (DC) electric field on the protein crystallization process has recently been investigated by crystallizing five globular proteins in a 1.3 V cm −1 DC field for 90 min.…”

Section: External Fieldsmentioning

confidence: 99%

Practical techniques for protein crystallization: additive assistance and external field intensification

Shao,

Han,

Tao

et al. 2024

CrystEngComm

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“…At present, many researchers have conducted studies on the regulation of LLPS, mainly by changing the composition of solvents 13,14 and using physical fields such as ultrasound, 11,15 laser, 16,17 and electric field. 18 The ability to effectively control the molecular self-assembly process of crystallization systems with LLPS phenomenon is critical to adjusting the qualities of crystal materials such as structure and function. Yet, the underlying mechanisms governing the transition from molecules to assemblies during LLPS have not been fully resolved.…”

Section: Introductionmentioning

confidence: 99%

“…Therefore, it is of great significance to fully achieve the precise regulation of LLPS for the treatment of some diseases and the preparation of crystal materials. At present, many researchers have conducted studies on the regulation of LLPS, mainly by changing the composition of solvents , and using physical fields such as ultrasound, , laser, , and electric field …”

Section: Introductionmentioning

confidence: 99%

Regulating of Liquid–Liquid Phase Separation and Molecular Self-Assembly through Selective Solvation

Huang,

Wang,

Wang

et al. 2023

Ind. Eng. Chem. Res.

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Effectively regulating the liquid–liquid phase separation (LLPS) phenomenon in the process of molecular self-assembly is critical for controlling the qualities of the final products. However, the underlying mechanisms of LLPS that greatly affect the transition from molecules to crystals have not been fully addressed. Here, target solvents with properties of solvation or selective solvation suppression were theoretically screened to regulate the emergence and elimination of LLPS. Quantitative analysis of molecular electrostatic potential surfaces (MESP) was first applied to screen the antisolvent with solvation suppressing effect. Selective solvation suppressing was revealed, and the evolution mechanism of self-assembly in the nucleation pathways with or without LLPS was explored by experiments. It was found that clusters with unique properties of core–shell structure with dispersion transition layer may be the key to the occurrence of LLPS. This further provides new insights for understanding LLPS, which is a typical case for nonclassical nucleation theory.

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Pulsed electric fields induce modulation of protein liquid–liquid phase separation

Abstract: The time-resolved dynamic assembly and the structures of protein liquid dense clusters (LDCs) were analyzed under pulsed electric fields (EFs) applying complementary polarized and depolarized dynamic light scattering (DLS/DDLS), optical...

Cited by 7 publications

References 52 publications

Voltage-calibrated, finely tunable protein assembly

Voltage-calibrated, finely tunable protein assembly

Practical techniques for protein crystallization: additive assistance and external field intensification

Regulating of Liquid–Liquid Phase Separation and Molecular Self-Assembly through Selective Solvation

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