Surface Functionalization Based on Protein Amyloid-like Aggregation★

doi:10.6023/A23060266

Acta Chimica Sinica ›› 2023, Vol. 81 ›› Issue (11): 1566-1576.DOI: 10.6023/A23060266 Previous Articles Next Articles

Special Issue: 庆祝《化学学报》创刊90周年合辑

Review

基于蛋白质类淀粉样聚集的表面功能化^★

伏成玉^a^,^b^,^c, 周星宇^a^,^b^,^c, 杨鹏^a^,^b^,^c^,^*()

a 陕西师范大学化学化工学院应用表面与胶体化学教育部重点实验室西安 710119
b 陕西师范大学化学化工学院西安市高分子软物质重点实验室西安 710119
c 陕西师范大学化学化工学院功能纤维与柔性智能织物国际联合研究中心西安 710119

投稿日期:2023-06-01 发布日期:2023-09-30

作者简介:

伏成玉, 2018年毕业于南京师范大学, 2019年至今陕西师范大学博士研究生在读, 研究方向为功能性织物的界面研究.

周星宇, 2021年毕业四川师范大学, 2021年至今陕西师范大学硕士研究生在读. 研究方向为类淀粉样界面改性.

杨鹏, 2006年北京化工大学高分子化学与物理博士毕业, 师从杨万泰院士. 之后赴德国马普研究所胶体与界面部、美国杜克大学和日本东京大学进行博士后研究. 2012年7月开始在陕西师范大学工作, 先后主持和完成国家自然科学基金委项目4项. 2022年获得国家自然科学基金委下属杰出青年科学基金资助. 2022年入选美国斯坦福大学发布的“全球2%顶尖科学家”榜单. 主要从事类淀粉样蛋白质组装及表界面改性的研究.

^†共同第一作者

^★庆祝《化学学报》创刊90周年.

基金资助:
国家杰出青年科学基金(52225301); 国家重点研发计划(2020YFA0710400); 国家重点研发计划(2020YFA0710402); 111计划(B14041); 中央高校基础研究基金(GK202305001); 陕西省创新能力支撑计划(2020TD-024); 陕西省国际科技合作项目(2022KWZ-24)

Surface Functionalization Based on Protein Amyloid-like Aggregation^★

Chengyu Fu^a^,^b^,^c, Xingyu Zhou^a^,^b^,^c, Peng Yang^a^,^b^,^c()

a Key Laboratory of Applied Surface and Colloid Chemistry (Ministry of Education), School of Chemistry and Chemical Engineering, Shaanxi Normal University, Xi’an 710119
b Xi’an Key Laboratory of Polymeric Soft Matter, School of Chemistry and Chemical Engineering, Shaanxi Normal University, Xi’an 710119
c International Joint Research Center on Functional Fiber and Soft Smart Textile, School of Chemistry and Chemical Engineering, Shaanxi Normal University, Xi’an 710119

Received:2023-06-01 Published:2023-09-30
Contact: *E-mail: yangpeng@snnu.edu.cn
About author:
^†These authors contributed equally to this work
^★Dedicated to the 90th anniversary of Acta Chimica Sinica.
Supported by:
National Science Foundation through Distinguished Young Scholars(52225301); National Key R&D Program of China(2020YFA0710400); National Key R&D Program of China(2020YFA0710402); 111 Project(B14041); Fundamental Research Funds for the Central Universities(GK202305001); Innovation Capability Support Program of Shaanxi Province(2020TD-024); International Science and Technology Cooperation Program of Shaanxi Province(2022KWZ-24)

Surface modification plays a pivotal role across various domains by conferring novel properties and heightened value to materials, all while preserving their inherent characteristics. However, a critical impediment stalling the broader utilization and advancement of advanced interface materials is the absence of a simple, environmentally friendly, universally applicable, colorless and transparent interface modification system. Since the initial reports of employing amyloid-like proteins for interface modification, this approach has garnered considerable attention and research within the academic community. Subsequently, an array of protein-based materials featuring diverse morphological structures such as nanofilms, nanofibers, large particle aggregates, hydrogels, aerogels, and more have emerged. This review commences by elucidating the fundamental principles underlying amyloid-like protein aggregation. Subsequently, it provides a comprehensive summary of its applications as a surface modification system in various domains including biomedical coatings, separation and dialysis, biomineralization, flexible electronics, smart fabrics, chemical catalysis and environmental pollutant removal. Furthermore, it discusses the current application directions and ultimately highlights the system's limitations, concluding with a prospective outlook on its future development.

Key words: surface/interface modification, amyloid-like protein, nanofilm

Cite this article

Chengyu Fu, Xingyu Zhou, Peng Yang. Surface Functionalization Based on Protein Amyloid-like Aggregation^★[J]. Acta Chimica Sinica, 2023, 81(11): 1566-1576.

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Fig. & Tab. 11

Figure 2. Schematic of chain relaxation-crystallization (from an amorphous nanofilm to extended and oriented crystals through edge-to-edge extension and face-to-face packing. Reproduced from Ref. [23] with permission from Wiley-VCH)

Figure 3. Four strategies of surface modification of amyloid-like protein and its universality and adhesion mechanism (Reprinted with permission from Ref. [25], Copyright 2021, American Chemical Society)

Figure 4. Application direction of amyloid-like protein system

Figure 5. (a) Design of functional antibacterial surface on medical titanium alloy surface. Reprinted with permission from Ref. [42], Copyright 2018, Applied Surface Science. (b) Schematic diagram of therapeutic effect of BC/PTL/Cu composite on bacterial infected wounds. (Reprinted with permission from Ref. [46], Copyright 2023, Carbohydrate Polymers)

Figure 6. Construction of HAp layers mediated by amyloid-like protein modification and the ectopic osteogenesis animal model (Reproduced from Ref. [52] with permission from American Chemical Society)

Figure 7. Construction of functional fabrics (Reproduced from Ref. [59], with permission from International Journal of Biological Macromolecules)

Figure 8. Application of amyloid-like protein aggregation in flexible devices (Reproduced from Ref. [61], all with permission from Wiley-VCH)

Figure 9. Amyloid-mediated photo/electrocatalysis research (Reproduced from Ref. [63], with permission from Wiley-VCH)

Figure 10. Surface modification of amyloid-like nanofilms for filtration membranes (Figure 10a, reprinted with permission from Ref. [66], Copyright 2022, American Chemical Society. Figure 10b, reprinted with permission from Ref. [67], Copyright 2021, Separation and Purification Technology)

Figure 11. Construction of amyloid-like protein to remove pollutants in water (Reproduced from Ref. [70], with permission from Chemical Engineering Journal)

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基于蛋白质类淀粉样聚集的表面功能化^★

Surface Functionalization Based on Protein Amyloid-like Aggregation^★

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基于蛋白质类淀粉样聚集的表面功能化★

Surface Functionalization Based on Protein Amyloid-like Aggregation★

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Abstract

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Fig. & Tab. 11

References 77

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基于蛋白质类淀粉样聚集的表面功能化^★

Surface Functionalization Based on Protein Amyloid-like Aggregation^★