Regulation of Biomineralization via Protein Assembling Scaffolds

Biomineralization is a biological process through which organisms produce mineralized structures to improve their adaptation to environmental challenges. In nature, biomineralization primarily contributes to the formation of hard tissues such as teeth and bone. This process is remarkably complex and involves the self-assembly of proteins into scaffolds that play critical regulatory roles. For instance, collagen molecules self-assemble into fibrils, and their unique quarter-staggered arrangement provides both a spatial template and a defined chemical microenvironment for the nucleation and growth of hydroxyapatite (HAp). Such precise regulation ensures the formation of highly ordered and functional mineralized structures in bone and dentin. This exquisite mechanism highlights the interaction between biological systems and mineralization, demonstrating the refinement of natural evolution and offering inspiration for the development of artificial biomimetic systems. In this review, we first discuss the structural characteristics of self-assembled scaffolds formed by three representative proteins, and their distinct structures provide diverse templates for mineral deposition. Subsequently, we analyze the mineralization mechanisms regulated by these protein scaffolds. Finally, we summarize recent advances in the field of artificial biomimetic mineralization, with particular emphasis on their applications and potential in tissue repair. This overview aims to promote the integration of assembly biopolymer science with advanced biomedical applications.