ArticleHua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology2021
Self-assembly and mineralization of full-length human amelogenin and its functional fragments
Article in Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 4 citations in OpenAlex.
- A Biomimetic Amelogenin-Fibronectin Fusion Protein with Dual Cell-Adhesive and Osteoinductive Functions for Alveolar Bone Defect Repair.Bioengineering (Basel, Switzerland) · 2026Article
- Advanced biomimetic mineralization approaches for enamel and dentin regeneration: a review.Odontology · 2026Review
- Amelogenin enhances the reparative competence of trauma-affected periodontal ligament stem cells: implications for tooth autotransplantation.BMC oral health · 2026Article
- Recombinant amelogenin peptide TRAP promoting remineralization of early enamel caries: AnFrontiers in physiology · 2023Article
- Application of Amorphous Calcium Phosphate Agents in the Prevention and Treatment of Enamel Demineralization.Frontiers in bioengineering and biotechnology · 2022Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
objectivesTo investigate the dynamic process of the self-assembly behaviors of a full-length human amelogenin (AM) and its functional fragments tyrosine-rich amelogenin peptide (TRAP) and leucine-rich amelogenin peptide(LRAP)
methodsThe full-length human AM and its functional fragments, TRAP and LRAP, were reassembled and purified
resultsWhen pH=8, the full-length human AM and TRAP assembly started spontaneously and formed "nanospheres" after 15 min.The nanospheres formed by TRAP existed independently, with a uniform size but without obvious internal structures. The full-length AM was assembled hierarchically, which formed "nanospheres" and further extended in all directions, formed a chain structure, and then aggregated into a net. The self-assembly behavior of LRAP was not obvious. Proteins mostly existed in the form of monomers without "nanosphere" formation. Only few oligomers were observed. The full-length AM was induced independently for 3 days to form rod-shaped HA crystals. TRAP and LRAP proteins were added, after 3 days the crystal elongation was obvious in the c axis, but the growth in plane A and plane B was poor.
conclusionsThe self-assembly and mineralization behaviors of full-length human AM, TRAP, and LRAP were consistent with the directional growth mechanism of HA crystals
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