Laser-Polarization-Induced Anisotropy Enhances Protein Crystallization.

Tien Chen, Hirotsugu Hiramatsu, Shuichi Toyouchi, Teruki Sugiyama

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Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed

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1 citing paper in PubMed.

Deciphering Amyloid Fibril Formation through Protein Concentration by Optical Trapping.JACS Au · 2025
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Authors and funding

4 authors.

Tien ChenDepartment of Applied Chemistry and Center for Emergent Functional Matter Science, National Yang Ming Chiao Tung University, Hsinchu, 300093, Taiwan.

Hirotsugu HiramatsuDepartment of Applied Chemistry and Center for Emergent Functional Matter Science, National Yang Ming Chiao Tung University, Hsinchu, 300093, Taiwan.

Shuichi ToyouchiResearch Institute for Light-induced Acceleration System (RILACS), Osaka Metropolitan University, Sakai, 599-8570, Japan.

Teruki SugiyamaDepartment of Applied Chemistry and Center for Emergent Functional Matter Science, National Yang Ming Chiao Tung University, Hsinchu, 300093, Taiwan.

Funding

KAKENHI Grant-in-Aid JP22H05138KAKENHI Grant-in-Aid JP22K20512Ministry of Education NSTC 111-2634-F-A49-007National Science and Technology Council NSTC 113-2113-M-A49-022National Science and Technology Council NSTC 113-2113-M-A49-023

6 · The paper itself

Abstract

Protein crystallization plays a critical role in structural biology and drug development, driving extensive research into its control. We present a novel approach for manipulating protein crystallization by controlling the anisotropy of the high-concentration domain (HCD) composed of hen egg-white lysozyme (HEWL) through laser polarization in optical trapping. The anisotropy of the HCD was assessed through fluorescence anisotropy measurements and polarized Raman spectroscopy. The results revealed that linear polarization significantly enhances crystallization efficiency by inducing anisotropy of the HCD and promoting nucleation. In contrast, circular polarization resulted in weak anisotropy with minimal crystallization efficiency. This study highlights the crucial role of protein molecule anisotropy in crystallization under optical trapping conditions, providing a new strategy to optimize laser conditions for various protein molecules and pave the way for the development of innovative crystallization techniques, potentially revolutionizing structural biology and drug discovery efforts.

Indexed as

LasersMuramidaseAnimalsAnisotropyChickensCrystallizationSpectrum Analysis, Ramanhen egg lysozymeMuramidaseAnisotropyFluorescence anisotropyLaser polarizationOptical trappingProtein crystallization

Identifiers

PMID40051228

DOI10.1002/anie.202501827

PMCPMC12087825

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