Amyloid-like ribbons of amelogenins in enamel mineralization

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

Research output: Contribution to journalArticlepeer-review

45 Citations (SciVal)


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.

Original languageEnglish
Article number23105
JournalScientific Reports
Publication statusPublished - 2016

Subject classification (UKÄ)

  • Chemical Sciences


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