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