Protein crystal regulation and harvest via electric field-based method

Yuan, Zhijie; Wu, Mengyuan; Meng, Yingshuang; Niu, Yuchao; Xiao, Wu; Ruan, Xuehua; He, Gaohong; Jiang, Xiaobin

doi:10.1016/j.coche.2021.100744

Cited by 5 publications

(3 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…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.

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 99%

Voltage-calibrated, finely tunable protein assembly

Lin

Masquelier

Sabeh

et al. 2023

J. R. Soc. Interface.

View full text Add to dashboard Cite

show abstract

“…Deep eutectic solvents (DESs) 36 and molecularly imprinted polymers (MIPs) 37 have also been applied to the field of protein crystallization in recent years with preeminent results. Generally, additives change the chemical environment of protein crystallization, while external fields (magnetic fields, 38 electric fields, 39 ultrasound fields, 40 shear, 41 and light fields 42 ) achieve distinctive effects on protein crystallization by introducing physical/chemical interactions or bring great energy. The strengthening effects of the external fields on protein crystallization were explored in the late 1990s, 43,44 but have shown strong development due to their extraordinary regulatory role in the protein crystallization process.…”

Section: Introductionmentioning

confidence: 99%

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

Shao,

Han,

Tao

et al. 2024

CrystEngComm

View full text Add to dashboard Cite

show abstract

“…Since proteins are investigated in aqueous solutions, the description of continuous EF perturbation must also account for electrochemical effects, including electrophoresis, charge separation and reduction, and entropic and polarization effects on the surrounding water molecules. While persistent efforts are underway to coherently describe the EF effect on the structure and activity of proteins and enzymes, the assistance of an external EF in the nucleation and tuned growth of better quality protein crystals has also been increasingly recognized for two decades now. − …”

Section: Introductionmentioning

confidence: 99%