Optically Controlled Construction of Three-Dimensional Protein Arrays

Qing Liu; Yu Zhou; Ahmed Shaukat; Zhuojun Meng; Daniella Kyllönen; Iris Seitz; Daniel Langerreiter; Kim Kuntze; Arri Priimagi; Lifei Zheng; Mauri A. Kostiainen

doi:10.1002/anie.202303880

Optically Controlled Construction of Three-Dimensional Protein Arrays

Qing Liu
, Yu Zhou
, Ahmed Shaukat
, Zhuojun Meng
, Daniella Kyllönen
, Iris Seitz
, Daniel Langerreiter
, Kim Kuntze
, Arri Priimagi
, Lifei Zheng^*
, Mauri A. Kostiainen^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Scientific › peer-review

14 Citations (Scopus)

12 Downloads (Pure)

Abstract

Protein crystallization is an important tool for structural biology and nanostructure preparation. Here, we report on kinetic pathway-dependent protein crystals that are controlled by light. Photo-responsive crystallites are obtained by complexing the model proteins with cationic azobenzene dyes. The crystalline state is readily switched to a dispersed phase under ultraviolet light and restored by subsequent visible-light illumination. The switching can be reversibly repeated for multiple cycles without noticeable structure deterioration. Importantly, the photo-treatment not only significantly increases the crystallinity, but creates crystallites at conditions where no ordered lattices are observed upon directly mixing the components. Further control over the azobenzene isomerization kinetics produces protein single crystals of up to ≈50 μm. This approach offers an intriguing method to fabricate metamaterials and study optically controlled crystallization.

Original language	English
Journal	Angewandte Chemie - International Edition
Volume	62
Issue number	28
DOIs	https://doi.org/10.1002/anie.202303880
Publication status	Published - 10 Jul 2023
Publication type	A1 Journal article-refereed

Funding

This work has received funding from the European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme (Grant Agreement No. 101002258). We acknowledge the funding from the Jane and Aatos Erkko Foundation, the Magnus Ehrnrooth Foundation, Tampere University Graduate School, the National Nature Science Foundation of China (No. 22277018), the Zhejiang Provincial Natural Science Foundation for Distinguished Young Scholar (LR23B030001), and Wenzhou Institute, University of Chinese Academy of Sciences (No. WIUCASQD2020015, No. WIUCASQD2022006, No. WIUCASQD2021048). We acknowledge the provision of facilities and technical support by Aalto University Bioeconomy Facilities and OtaNano‐Nanomicroscopy Center (Aalto‐NMC). The authors thank Jani Seitsonen from the Department of Applied Physics, Aalto University, for the support in cryo‐TEM measurements. This work was carried out under the Academy of Finland's Centers of Excellence Programme, Life Inspired Hybrid Materials (LIBER) Center of Excellence (2022–2029), and the Flagship Programme PREIN (No. 320165).

Keywords

Azobenzene
Crystallization
Kinetic Pathway
Photo Responsiveness
Protein Cage

Publication forum classification

Publication forum level 3

ASJC Scopus subject areas

Catalysis
General Chemistry

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10.1002/anie.202303880Licence: CC BY

Angew Chem Int Ed - 2023 - Liu - Optically Controlled Construction of Three‐Dimensional Protein ArraysFinal published version, 1.69 MBLicence: CC BY

https://urn.fi/URN:NBN:fi:tuni-202308017385Licence: CC BY

Cite this

@article{7d31350333ed47f5be66b27082c88828,

title = "Optically Controlled Construction of Three-Dimensional Protein Arrays",

abstract = "Protein crystallization is an important tool for structural biology and nanostructure preparation. Here, we report on kinetic pathway-dependent protein crystals that are controlled by light. Photo-responsive crystallites are obtained by complexing the model proteins with cationic azobenzene dyes. The crystalline state is readily switched to a dispersed phase under ultraviolet light and restored by subsequent visible-light illumination. The switching can be reversibly repeated for multiple cycles without noticeable structure deterioration. Importantly, the photo-treatment not only significantly increases the crystallinity, but creates crystallites at conditions where no ordered lattices are observed upon directly mixing the components. Further control over the azobenzene isomerization kinetics produces protein single crystals of up to ≈50 μm. This approach offers an intriguing method to fabricate metamaterials and study optically controlled crystallization.",

keywords = "Azobenzene, Crystallization, Kinetic Pathway, Photo Responsiveness, Protein Cage",

author = "Qing Liu and Yu Zhou and Ahmed Shaukat and Zhuojun Meng and Daniella Kyll{\"o}nen and Iris Seitz and Daniel Langerreiter and Kim Kuntze and Arri Priimagi and Lifei Zheng and Kostiainen, \{Mauri A.\}",

note = "Funding Information: This work has received funding from the European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme (Grant Agreement No. 101002258). We acknowledge the funding from the Jane and Aatos Erkko Foundation, the Magnus Ehrnrooth Foundation, Tampere University Graduate School, the National Nature Science Foundation of China (No. 22277018), the Zhejiang Provincial Natural Science Foundation for Distinguished Young Scholar (LR23B030001), and Wenzhou Institute, University of Chinese Academy of Sciences (No. WIUCASQD2020015, No. WIUCASQD2022006, No. WIUCASQD2021048). We acknowledge the provision of facilities and technical support by Aalto University Bioeconomy Facilities and OtaNano‐Nanomicroscopy Center (Aalto‐NMC). The authors thank Jani Seitsonen from the Department of Applied Physics, Aalto University, for the support in cryo‐TEM measurements. This work was carried out under the Academy of Finland's Centers of Excellence Programme, Life Inspired Hybrid Materials (LIBER) Center of Excellence (2022–2029), and the Flagship Programme PREIN (No. 320165). Publisher Copyright: {\textcopyright} 2023 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.",

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AU - Liu, Qing

AU - Zhou, Yu

AU - Shaukat, Ahmed

AU - Meng, Zhuojun

AU - Kyllönen, Daniella

AU - Seitz, Iris

AU - Langerreiter, Daniel

AU - Kuntze, Kim

AU - Priimagi, Arri

AU - Zheng, Lifei

AU - Kostiainen, Mauri A.

N1 - Funding Information: This work has received funding from the European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme (Grant Agreement No. 101002258). We acknowledge the funding from the Jane and Aatos Erkko Foundation, the Magnus Ehrnrooth Foundation, Tampere University Graduate School, the National Nature Science Foundation of China (No. 22277018), the Zhejiang Provincial Natural Science Foundation for Distinguished Young Scholar (LR23B030001), and Wenzhou Institute, University of Chinese Academy of Sciences (No. WIUCASQD2020015, No. WIUCASQD2022006, No. WIUCASQD2021048). We acknowledge the provision of facilities and technical support by Aalto University Bioeconomy Facilities and OtaNano‐Nanomicroscopy Center (Aalto‐NMC). The authors thank Jani Seitsonen from the Department of Applied Physics, Aalto University, for the support in cryo‐TEM measurements. This work was carried out under the Academy of Finland's Centers of Excellence Programme, Life Inspired Hybrid Materials (LIBER) Center of Excellence (2022–2029), and the Flagship Programme PREIN (No. 320165). Publisher Copyright: © 2023 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH.

PY - 2023/7/10

Y1 - 2023/7/10

N2 - Protein crystallization is an important tool for structural biology and nanostructure preparation. Here, we report on kinetic pathway-dependent protein crystals that are controlled by light. Photo-responsive crystallites are obtained by complexing the model proteins with cationic azobenzene dyes. The crystalline state is readily switched to a dispersed phase under ultraviolet light and restored by subsequent visible-light illumination. The switching can be reversibly repeated for multiple cycles without noticeable structure deterioration. Importantly, the photo-treatment not only significantly increases the crystallinity, but creates crystallites at conditions where no ordered lattices are observed upon directly mixing the components. Further control over the azobenzene isomerization kinetics produces protein single crystals of up to ≈50 μm. This approach offers an intriguing method to fabricate metamaterials and study optically controlled crystallization.

AB - Protein crystallization is an important tool for structural biology and nanostructure preparation. Here, we report on kinetic pathway-dependent protein crystals that are controlled by light. Photo-responsive crystallites are obtained by complexing the model proteins with cationic azobenzene dyes. The crystalline state is readily switched to a dispersed phase under ultraviolet light and restored by subsequent visible-light illumination. The switching can be reversibly repeated for multiple cycles without noticeable structure deterioration. Importantly, the photo-treatment not only significantly increases the crystallinity, but creates crystallites at conditions where no ordered lattices are observed upon directly mixing the components. Further control over the azobenzene isomerization kinetics produces protein single crystals of up to ≈50 μm. This approach offers an intriguing method to fabricate metamaterials and study optically controlled crystallization.

KW - Azobenzene

KW - Crystallization

KW - Kinetic Pathway

KW - Photo Responsiveness

KW - Protein Cage

U2 - 10.1002/anie.202303880

DO - 10.1002/anie.202303880

M3 - Article

AN - SCOPUS:85158842275

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 28

ER -

Optically Controlled Construction of Three-Dimensional Protein Arrays

Abstract

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Keywords

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