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Amyloid-like ribbons of amelogenins in enamel mineralization

Carneiro, Karina M M (author)
University of California System
Zhai, Halei (author)
University of California System
Zhu, Li (author)
University of California System
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Horst, Jeremy A (author)
University of California System
Sitlin, Melody (author)
University of California System
Nguyen, Mychi (author)
University of California System
Wagner, Martin (author)
Bruker
Simpliciano, Cheryl (author)
University of California System
Milder, Melissa (author)
University of California System
Chen, Chun-Long (author)
Lawrence Berkeley National Laboratory
Ashby, Paul (author)
Pacific Northwest National Laboratory
Svensson Bonde, Johan (author)
Lund University,Lunds universitet,Tillämpad biokemi,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Pure and Applied Biochemistry,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
Li, Wu (author)
University of California System
Habelitz, Stefan (author)
University of California System
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 (creator_code:org_t)
2016-03-24
2016
English.
In: Scientific Reports. - : Springer Science and Business Media LLC. - 2045-2322. ; 6
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Subject headings

NATURVETENSKAP  -- Kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences (hsv//eng)

Publication and Content Type

art (subject category)
ref (subject category)

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