Related Experiment Video
Updated: Jun 27, 2025
Isolation of Whole Cell Protein Lysates from Mouse Facial Processes and Cultured Palatal Mesenchyme Cells for Phosphoprotein Analysis
Published on: April 1, 2022
Phosphorylation of collagen fibrils enhances intrafibrillar mineralization and dentin remineralization
Bo Zheng1, Luyi Zhao1, Lelu Chen2
1Stomatology Hospital, School of Stomatology, Zhejiang University School of Medicine, Clinical Research Center for Oral Diseases of Zhejiang Province, Key Laboratory of Oral Biomedical Research of Zhejiang Province, Cancer Center of Zhejiang University, Hangzhou 310006, China. shaocy@zju.edu.cn.
Abstract:
The hierarchical assembly of nanoapatite within a type I collagen matrix was achieved through biomimetic mineralization in vitro, cooperatively regulated by non-collagenous proteins and small biomolecules. Here, we demonstrated that IP6 could significantly promote intrafibrillar mineralization in two- and three-dimensional collagen models through binding to collagen fibrils via hydrogen bonds (the interaction energy ∼10.21 kJ mol-1), as confirmed by the FTIR spectra and isothermal experimental results. In addition, we find that IP6 associated with dental collagen fibrils can also enhance the remineralization of calcium-depleted dentin and restore its mechanical properties similar to the natural dentin within 4 days. The promoting effect is mainly due to the chemical modification of IP6, which alters the interfacial physicochemical properties of collagen fibrils, strengthening the interaction of calcium phosphate minerals and mineral ions with collagen fibrils. This strategy of interfacial regulation to accelerate the mineralization of collagen fibrils is essential for dental repair and the development of a clinical product for the remineralization of hard tissue.
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