3D Printing of Proteins Via Temperature‐Dependent Amyloid Aggregation

Abstract 3D printing of protein materials for creating bioactive scaffolds has attracted significant interest. However, achieving controllable and stable printing while replicating the ordered structure found in natural protein materials remains a key challenge. Herein, a universally applicable temperature‐dependent protein aggregation (TPA) strategy is reported to manipulate the unfolding, relaxation, and reorganization of protein chains to enable the 3D printing of amyloid‐like proteins. The disruption of internal disulfide bonds induces the unfolding and relaxation of protein, leading to the formation of an amorphous protein sol through chain entanglement as primary cross‐linking points. These relaxed protein chains further aggregate through conformational transition to initiate amyloid‐like protein aggregation rich in β‐sheet structures at high temperature, resulting in a protein gel with β‐sheet nanocrystals serving as secondary cross‐linking points. This gel facilitates the stable and precise extrusion‐based 3D printing of proteinaceous scaffolds with a hierarchically ordered structure. The biomedical potential of this 3D‐printed protein scaffold is preliminarily validated through its biomineralization capability and following application in bone tissue regeneration using rat skull defect models. This strategy demonstrates a facile approach for the controllable structural aggregation of proteins in vitro and holds great potential in the field of protein‐based scaffolds.

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Publication Details

Journal
Advanced Functional Materials
Published
2024-12-01
DOI
https://doi.org/10.1002/adfm.202420569
Citations
12
Primary Topic
3D Printing in Biomedical Research
Type
article
Field-Weighted Citation Impact
2.21

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article

3D Printing of Proteins Via Temperature‐Dependent Amyloid Aggregation

Wenrui Ji, Chengyu Fu, Yingtao Gao, Zhengge Wang et al.
12 citations
Advanced Functional Materials
3D Printing in Biomedical Research
2.21
article

3D Printing of Proteins Via Temperature‐Dependent Amyloid Aggregation

Wenrui Ji, Chengyu Fu, Yingtao Gao, Zhengge Wang, Yanyun Pang, Xu Zhang, Jinhua Song, Hui Zhou, Peng Yang, Zhaofang Huang, Min Li, Jinglin Wang, Yong‐Chun Liu, Xingyu Zhou, Jian Zhao, Jinrui Zhang, Jianing Ma, Bowen Hu
article en
12 citations

Abstract

Abstract 3D printing of protein materials for creating bioactive scaffolds has attracted significant interest. However, achieving controllable and stable printing while replicating the ordered structure found in natural protein materials remains a key challenge. Herein, a universally applicable temperature‐dependent protein aggregation (TPA) strategy is reported to manipulate the unfolding, relaxation, and reorganization of protein chains to enable the 3D printing of amyloid‐like proteins. The disruption of internal disulfide bonds induces the unfolding and relaxation of protein, leading to the formation of an amorphous protein sol through chain entanglement as primary cross‐linking points. These relaxed protein chains further aggregate through conformational transition to initiate amyloid‐like protein aggregation rich in β‐sheet structures at high temperature, resulting in a protein gel with β‐sheet nanocrystals serving as secondary cross‐linking points. This gel facilitates the stable and precise extrusion‐based 3D printing of proteinaceous scaffolds with a hierarchically ordered structure. The biomedical potential of this 3D‐printed protein scaffold is preliminarily validated through its biomineralization capability and following application in bone tissue regeneration using rat skull defect models. This strategy demonstrates a facile approach for the controllable structural aggregation of proteins in vitro and holds great potential in the field of protein‐based scaffolds.

Advanced Functional MaterialsVol. 35(14)
Shandong University (CN), Tianjin Medical University (CN), Shaanxi Normal University (CN)
Innovative Research Group Project of the National Natural Science Foundation of China, Natural Science Foundation of Shaanxi Province, National Key Research and Development Program of China, Fundamental Research Funds for the Central Universities, National Science Fund for Distinguished Young Scholars, Key Science and Technology Program of Shaanxi Province, Science and Technology Support Plan for Youth Innovation of Colleges and Universities of Shandong Province of China
Openalex Percentile: Top 12%
3D Printing in Biomedical Research
2.21
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