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Structure-Property Correlation in Genetically-Engineered Mouse Enamel

Published online by Cambridge University Press:  02 July 2020

Hanson Fong ,
Daniel Heidel ,
Mehmet Sarikaya ,
Michael Paine ,
Wen Lou ,
Shane N. White  and
Malcolm L. Snead
Hanson Fong
Affiliation:
Materials Science & Engineering, University of Washington, Seattle, WA, 98105
Daniel Heidel
Affiliation:
Materials Science & Engineering, University of Washington, Seattle, WA, 98105
Mehmet Sarikaya
Affiliation:
Materials Science & Engineering, University of Washington, Seattle, WA, 98105
Michael Paine
Affiliation:
Center for Craniofacial Molecular Biology, University of Southern California, Los Angeles, CA, 90033
Wen Lou
Affiliation:
Center for Craniofacial Molecular Biology, University of Southern California, Los Angeles, CA, 90033
Shane N. White
Affiliation:
School of Dentistry, University of California, Los Angeles, CA, 90095
Malcolm L. Snead
Affiliation:
Center for Craniofacial Molecular Biology, University of Southern California, Los Angeles, CA, 90033
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Abstract

Dental enamel is the most durable bioceramics produced by a vertebrate as it is designed to perform masticatory functions throughout its lifetime. The understanding of the mechanism of enamel formation and effects of proteins during the biomineralization process are fundamental issues, essential for both potential enamel regeneration and as a base for synthesis, via self-assembly, of biomimetic composites.

The biomineralization process of enamel is carried out by ameloblast cells that line the inner enamel epithelium and secrete an extracellular protein matrix onto a mineralized dentin surface at the dentin-enamel junction (DEJ). A major matrix protein, amelogenin, is believed to regulate the mineralization of hydroxyapatite (HAP) in the enamel tissue. It has been shown to undergo self-assembly in vitro and in vivo to form nanospheres of ∼20nm in diameter. Previous TEM studies have shown that the nanospheres align along the length (c-axis) of hydroxyapatite (HA) crystals. There are two domains, namely A (residues 1-42) and B (residues 157-173), that control the self-assembly behavior of the nanospheres.

Type
Biological Microanalysis
Information
Microscopy and Microanalysis , Volume 7 , Issue S2: Proceedings: Microscopy & Microanalysis 2001, Microscopy Society of America 59th Annual Meeting, Microbeam Analysis Society 35th Annual Meeting, Long Beach, California August 5-9, 2001 , August 2001 , pp. 992 - 993
Copyright
Copyright © Microscopy Society of America 2001

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References

1. Fong, H.et al., Mater. Sci. & Eng.-C, 7, 119 (2000).CrossRefGoogle Scholar

2. Paine, Met al., J. of Sir. Biol, in press (2001).Google Scholar

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4. Fong, H.et al., submitted (2001).Google Scholar

5. Supported by NIDCR under Grant #s. DE12420, DE06988, and DEI 1704.Google Scholar