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Updated: Aug 15, 2025

Development of Amelogenin-chitosan Hydrogel for In Vitro Enamel Regrowth with a Dense Interface
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Calcium interactions in amelogenin-derived peptide assembly.

Jing Zhang1,2,3, Yushi Bai4, Jian Wang1

  • 1School of Life Science and Technology, ShanghaiTech University, Shanghai, China.

Frontiers in Physiology
|January 2, 2023
PubMed
Summary

This study reveals how phosphorylated amelogenin peptides self-assemble with calcium ions. These interactions are crucial for forming the mineral structures in developing mammalian enamel.

Keywords:
SSNMRamelogeninassemblymineral ionsphosphorylation

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Area of Science:

  • Biomineralization
  • Structural Biology
  • Biochemistry

Background:

  • Phosphorylation of serine residues is key in mineralized tissue evolution.
  • Amelogenin is abundant in enamel development, influencing apatite fiber structure.
  • A 14-residue peptide (14P2) mediates amelogenin assembly and contains phosphoserine (Ser16).

Purpose of the Study:

  • To investigate the self-assembly of 14P2 and its phosphorylated form (p14P2) with calcium and phosphate ions.
  • To elucidate the structural details of these self-assemblies using solid-state Nuclear Magnetic Resonance (SSNMR).
  • To understand the role of calcium ions in amelogenin self-assembly during early enamel development.

Main Methods:

  • Investigated 14P2 and p14P2 at pH 6.0 with varying calcium and phosphate concentrations.
  • Utilized solid-state Nuclear Magnetic Resonance (SSNMR) 31P PITHIRDS-CT experiments.
  • Combined SSNMR data with other experimental results.

Main Results:

  • Both 14P2 and p14P2 self-assemble into amyloid-like conformations with distinct structural differences.
  • In the presence of calcium, the distance between 31P in p14P2 assemblies is 4.4 ± 0.2Å.
  • SSNMR suggests p14P2 assemblies adopt a parallel in-register beta-sheet conformation.
  • Calcium ions likely bridge adjacent peptide chains by interacting with Ser16 phosphate and Glu18 carboxylate.

Conclusions:

  • Amelogenin-derived peptides can self-assemble into ordered structures.
  • Divalent calcium ions play a critical role in mediating the assembly of phosphorylated amelogenin peptides.
  • These findings offer insights into the mechanism of amelogenin self-assembly in early enamel formation.