Preparation and Characterization of Crystalline Hydroxyapatite Induced by Self-Assembled Peptide and the Potential Application in Remineralizing Dentin

The generation of mineral crystals on the implant surface under physiological conditions is an efficient way to repair defects in hard tissues. However, there is still a challenge to mimic the complicated structure of hard tissue with well bonding stability. Herein, a peptide sequence: Leu-Asp-Asp-Try-Glu-Glu-Ser-Cys is designed. The peptide forms a self-assembled peptide (SAP) coating at the solid/water interface via a facile and rapid process. The abundant functional groups on the SAP coating can be utilized to bind with calcium ions trough chelation, which may facilitate the formation of c-axis hydroxyapatite crystals. Owing to the amyloid adhesion properties, a c-axis hydroxyapatite layer with low wear extent and well bonding robustness can be integrated with virtually arbitrary material irrespective of their size and morphology, even hard tissues such as dentin. This suggests that the facile process may hold a great potential application in repairing hard tissue and designing complex materials.

Automated summary

By designing a specific peptide sequence to form a self-assembled peptide (SAP) coating, utilizing its abundant functional groups to bind with calcium ions, the formation of c-axis hydroxyapatite crystals is facilitated.