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Amelogenin proteolysis orchestrates functional amyloid pathways in enamel development.

Emerson Tavares de Sousa1, Larry Ackerman2, Johan Svensson Bonde3

  • 1Department of Preventive and Restorative Dental Sciences, School of Dentistry, University of California, San Francisco, USA.

Matrix Biology : Journal of the International Society for Matrix Biology
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Summary

Amelogenin protein assembly into nanoribbons, crucial for enamel formation, is clarified. Proteolytic processing by MMP20 regulates this functional amyloid pathway, enabling controlled biomineralization.

Keywords:
AmelogenesisEnamel MatrixProtein-guided mineralizationProtein-protein interactionsß-sheet nanostructures

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Area of Science:

  • Biochemistry
  • Biomineralization
  • Protein self-assembly

Background:

  • Amelogenin is the primary protein in developing enamel, forming structures for apatite growth.
  • Its self-assembly into nanoribbons resembles functional amyloids, but mechanisms are unclear.

Purpose of the Study:

  • To elucidate the molecular mechanisms of amelogenin (rH174) and its MMP20 cleavage products' assembly pathways.
  • To investigate how proteolytic processing influences amelogenin's supramolecular organization and enamel matrix formation.

Main Methods:

  • Atomic force microscopy (AFM)
  • Transmission electron microscopy (TEM)
  • Spectroscopic analyses
  • Studied full-length rH174 and C-terminally truncated rH146, including cross-seeding experiments.

Main Results:

  • Both rH174 and rH146 assemble via nucleated conformational conversion into β-sheet-rich nanoribbons.
  • rH146 shows rapid nucleation and maturation, while rH174 has a delayed pathway.
  • Cross-seeding accelerates rH174 assembly, mimicking in vivo conditions.
  • The MMP20 cleavage product TRAP does not form nanoribbons, altering the pathway.

Conclusions:

  • Proteolysis-triggered assembly pathways regulate amelogenin's supramolecular structure for enamel biomineralization.
  • Amelogenin functions as a tunable vertebrate functional amyloid.
  • MMP20 processing controls matrix formation, preventing premature crystal fusion during amelogenesis.