Strategies and Applications for Supramolecular Protein Self-Assembly

Supramolecular chemistry achieves higher-order molecular self-assembly through non-covalent interactions. Utilizing supramolecular methods to explore the polymorphism of proteins, the building blocks of life, from a "bottom-up" perspective is essential for constructing diverse and functional biomaterials. In recent years, significant progress has been achieved in the design strategies and functional applications of supramolecular protein self-assembly, becoming a focal point for researchers. This paper reviews classical supramolecular strategies driving protein self-assembly, including electrostatic interactions, metal coordination, hydrogen bonding, hydrophobic interactions, host-guest interactions, and other mechanisms. We discuss how these supramolecular interactions regulate protein assembly processes and highlight protein supramolecular assemblies ' unique structural and functional advantages in constructing artificial photosynthetic systems, protein hydrogels, bio-delivery systems, and other functional materials. The enormous potential and significance of supramolecular protein materials are elucidated. Finally, the challenges in preparing and applying protein supramolecular assemblies are summarized, and future development directions are projected. Supramolecular hierarchical protein self-assembly is vital for constructing diverse and functional biomaterials, as well as to explore information exchange and cooperation between proteins. In this paper, the classical supramolecular protein assembly construction strategies and the flexible regulaion of assemblies are summarized and analyzed. In addition, the applications and the enormous potential and significance of supramolecular protein materials are also reviewed. image