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Structural changes in amelogenin upon self-assembly and mineral interactions.

E Beniash1, J P Simmer, H C Margolis

  • 1Department of Oral Biology, University of Pittsburgh, School of Dental Medicine, Center for Craniofacial Regeneration, McGowan Institute for Regenerative Medicine, Bioengineering, Swanson School of Engineering, 589 Salk Hall, 3501 Terrace Street, Pittsburgh, PA 15261, USA. ebeniash@pitt.edu

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Amelogenin protein undergoes structural changes with pH, forming ordered structures essential for dental enamel biomineralization. Interactions with minerals reduce this protein’s organization, revealing its flexibility in interacting with enamel components.

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Area of Science:

  • Biochemistry
  • Biomineralization
  • Materials Science

Background:

  • Amelogenin is the primary protein in developing dental enamel.
  • It plays a vital role in the formation and organization of dental enamel.
  • Amelogenin's solubility and self-assembly are pH-dependent.

Purpose of the Study:

  • To investigate the pH-triggered structural assembly of recombinant porcine amelogenin (rP172).
  • To examine the interactions between rP172 and calcium phosphate mineral phases.
  • To elucidate the role of amelogenin structure in enamel biomineralization.

Main Methods:

  • Fourier Transform Infrared Spectroscopy (FTIRS) was employed.
  • Studies focused on pH-induced assembly of rP172.
  • Interactions with hydroxyapatite and in situ apatitic mineral were analyzed.

Main Results:

  • At pH 3.0, rP172 was in an unfolded, disordered state.
  • Increasing pH promoted structural ordering, with increased β-sheet structures and decreased random coil.
  • Mineral interactions reduced the structural organization of amelogenin.

Conclusions:

  • Amelogenin exhibits pH-dependent structural transitions, forming ordered structures at physiological pH.
  • The protein possesses structural flexibility to interact with both forming and mature mineral phases.
  • These findings offer insights into the significance of amelogenin-mineral interactions during enamel biomineralization.