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Review | Publishing Language: Chinese | Open Access

Protein Self-assembly: from Single-Molecule Design to Multidimensional Supramolecular Assembly

Mingyang SUN Jiachen ZANGTuo ZHANGGuanghua ZHAOChenyan LÜ ( )
College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China
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Abstract

Protein self-assembly is a ubiquitous phenomenon in nature. Recent studies have revealed that protein assemblies, with their diverse functions and characteristics, demonstrate significant potential for applications in life science, material science, and food nutrition. This review systematically outlines key strategies in the field of protein self-assembly and the application of multidimensional protein assemblies. Through rational design and engineering, protein subunits or molecules can form zero-dimensional, one-dimensional, two-dimensional, and three-dimensional structures via covalent and non-covalent interactions. Current strategies for protein self-assembly primarily include symmetric fusion expression, computational de novo design, and key interface design. These approaches enable the construction of multidimensional protein assemblies ranging from zero to three dimensions, with broad application prospects in areas such as active substance encapsulation and delivery, artificial light-harvesting and photocatalytic systems, and biocatalysis. This article comprehensively reviews the design strategies and application of protein self-assembly, which not only enhances the understanding of natural protein assembly mechanisms but also provides theoretical support and methodological references for developing novel biomaterials and bionic systems. It holds great significance for advancing synthetic biology, nanobiotechnology, and sustainable materials development.

CLC number: Q518.3 Document code: A Article ID: 1002-6630(2025)24-0321-14

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Food Science
Pages 321-334

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Cite this article:
SUN M, ZANG J, ZHANG T, et al. Protein Self-assembly: from Single-Molecule Design to Multidimensional Supramolecular Assembly. Food Science, 2025, 46(24): 321-334. https://doi.org/10.7506/spkx1002-6630-20250710-081

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Received: 10 July 2025
Published: 25 December 2025
© Beijing Academy of Food Sciences 2025.

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).