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Title: Amyloid-like ribbons of amelogenins in enamel mineralization

Journal Article · · Scientific Reports
DOI:https://doi.org/10.1038/srep23105· OSTI ID:1253122
 [1];  [1];  [1];  [1];  [1];  [1];  [2];  [1];  [1];  [3];  [4];  [5];  [1];  [1]
  1. Univ. of California, San Francisco, CA (United States)
  2. Bruker Nano Surfaces Division, Santa Barbara, CA (United States)
  3. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  4. Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
  5. Lund Univ. (Sweden)
+ Show Author Affiliations

We report that 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. Lastly, 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.

Research Organization:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Organization:
USDOE
Grant/Contract Number:
AC02-05CH11231; AC05-76RL01830
OSTI ID:
1253122
Journal Information:
Scientific Reports, Vol. 6; ISSN 2045-2322
Publisher:
Nature Publishing GroupCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 67 works
Citation information provided by
Web of Science

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Cited By (12)

Protein disorder–order interplay to guide the growth of hierarchical mineralized structures journal June 2018
A Review of the Role of Amelogenin Protein in Enamel Formation and Novel Experimental Techniques to Study its Function journal October 2019
M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils journal January 2018
Posttranslational Amelogenin Processing and Changes in Matrix Assembly during Enamel Development journal October 2017
Hierarchical Biomineralization: from Nature's Designs to Synthetic Materials for Regenerative Medicine and Dentistry journal June 2018
Biomimetic Remineralization of Carious Lesions by Self-Assembling Peptide journal March 2017
Dental Enamel Formation and Implications for Oral Health and Disease journal July 2017
Alzheimer’s Amyloid-β is an Antimicrobial Peptide: A Review of the Evidence journal March 2018
Peptide-Based Bioinspired Approach to Regrowing Multilayered Aprismatic Enamel journal March 2018
Elastin-Like Protein, with Statherin Derived Peptide, Controls Fluorapatite Formation and Morphology journal June 2017
Predicting Amyloidogenic Proteins in the Proteomes of Plants journal October 2017
Amyloids and prions in plants: Facts and perspectives journal September 2017

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
Phosphoproteins
Protein aggregation