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中华口腔医学研究杂志(电子版) ›› 2026, Vol. 20 ›› Issue (04) : 253 -261. doi: 10.3877/cma.j.issn.1674-1366.2026.04.002

生物材料专栏·专家论坛

淀粉样蛋白介导的生物矿化:从矿化机制到仿生硬组织修复
叶杨杨1, 张旭2,()   
  1. 1浙江大学医学院附属口腔医院,浙江大学口腔医学院,浙江省口腔疾病临床医学研究中心,全省口腔生物医学重点实验室,杭州 310000
    2天津医科大学口腔医学院·口腔医院,天津市口腔软硬组织修复再生重点实验室,天津医科大学口腔研究所,天津 300070
  • 收稿日期:2026-06-18 出版日期:2026-08-01
  • 通信作者: 张旭

Functional amyloids in biomineralization: From molecular mechanisms to biomimetic hard tissue repair

Yangyang Ye1, Xu Zhang2,()   

  1. 1Stomatology Hospital, School of Stomatology, Zhejiang University School of Medicine, Zhejiang Provincial Clinical Research Center for Oral Diseases, Zhejiang Key Laboratory of Oral Biomedical, Hangzhou 310000, China
    2Tianjin Medical University School and Hospital of Stomatology & Tianjin Key Laboratory of Oral Soft and Hard Tissues Restoration and Regeneration, Tianjin 300070, China
  • Received:2026-06-18 Published:2026-08-01
  • Corresponding author: Xu Zhang
  • Supported by:
    National Key R & D Program of China(2022YFC2405900, 2022YFC2405902)
引用本文:

叶杨杨, 张旭. 淀粉样蛋白介导的生物矿化:从矿化机制到仿生硬组织修复[J/OL]. 中华口腔医学研究杂志(电子版), 2026, 20(04): 253-261.

Yangyang Ye, Xu Zhang. Functional amyloids in biomineralization: From molecular mechanisms to biomimetic hard tissue repair[J/OL]. Chinese Journal of Stomatological Research(Electronic Edition), 2026, 20(04): 253-261.

生物矿化是指生物体通过细胞与有机基质的共同作用,在受控的微环境中生成无机矿物质的生物学过程,它是骨骼、牙齿和贝壳等硬组织形成的基础。在此过程中,矿物质的成核、晶体生长和层级组装受到特定蛋白质的严格调控。近年来,功能性淀粉样蛋白因其独特的结构特征、卓越的机械性能及聚集特性,在生物矿化中的调控作用备受关注。越来越多的研究表明,功能性淀粉样蛋白及其前体内在无序蛋白在矿物成核、晶体生长及矿物相的层级组装方面发挥着关键作用。淀粉样蛋白不仅在阿尔茨海默病等神经退行性疾病中被广泛研究,其独特的自组装特性也为生物材料、再生医学和纳米技术开辟了新的机遇。本文系统综述了生物矿化的经典与非经典结晶理论、淀粉样蛋白的结构特性及其诱导矿化的分子机制,并探讨了淀粉样蛋白在牙体、骨等硬组织仿生修复中的研究进展。

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.

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