Amyloid-like ribbons of amelogenins in enamel mineralization

Research output: Contribution to journalArticle

Abstract

Enamel, the outermost layer of teeth, is an acellular mineralized tissue that cannot regenerate; the mature tissue is composed of high aspect ratio apatite nanocrystals organized into rods and inter-rod regions. Amelogenin constitutes 90% of the protein matrix in developing enamel and plays a central role in guiding the hierarchical organization of apatite crystals observed in mature enamel. To date, a convincing link between amelogenin supramolecular structures and mature enamel has yet to be described, in part because the protein matrix is degraded during tissue maturation. Here we show compelling evidence that amelogenin self-assembles into an amyloid-like structure in vitro and in vivo. We show that enamel matrices stain positive for amyloids and we identify a specific region within amelogenin that self-assembles into β-sheets. We propose that amelogenin nanoribbons template the growth of apatite mineral in human enamel. This is a paradigm shift from the current model of enamel development.

Details

Authors
  • Karina M M Carneiro
  • Halei Zhai
  • Li Zhu
  • Jeremy A Horst
  • Melody Sitlin
  • Mychi Nguyen
  • Martin Wagner
  • Cheryl Simpliciano
  • Melissa Milder
  • Chun-Long Chen
  • Paul Ashby
  • Johan Svensson Bonde
  • Wu Li
  • Stefan Habelitz
Organisations
External organisations
  • Bruker
  • Lawrence Berkeley National Laboratory
  • University of California System
  • Pacific Northwest National Laboratory
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Chemical Sciences
Original languageEnglish
Article number23105
JournalScientific Reports
Volume6
Publication statusPublished - 2016
Publication categoryResearch
Peer-reviewedYes