Biomineralization is the biological process by which organisms produce inorganic minerals within a regulated microenvironment through the coordinated actions of cells and the extracellular organic matrix. It underpins the formation of mineralized tissues such as bone, teeth, and shells. During this process, mineral nucleation, crystal growth, and hierarchical assembly are tightly regulated by specific matrix proteins. In recent years, functional amyloid proteins have attracted considerable attention for their regulatory role in biomineralization due to their unique structure, remarkable mechanical stability, and self-assembly capability. Increasing evidence indicates that functional amyloid proteins, together with their intrinsically disordered precursor proteins, play critical roles in controlling mineral nucleation, crystal growth, and the hierarchical organization of mineral phases in vivo. Although amyloid proteins are best known for their association with neurodegenerative diseases such as Alzheimer's disease, their unique self-assembly behavior has also opened new opportunities in biomaterials, regenerative medicine, and nanotechnology. This review systematically summarizes both classical and non-classical theories of biomineralization, discusses the structural characteristics of amyloid proteins and the molecular mechanisms underlying amyloid-mediated mineralization, and highlights recent advances in the application of amyloid proteins for the biomimetic regeneration of mineralized tissues, particularly bone and dental hard tissues.