Publication Date:
2005-03-05
Description:
Although both tooth enamel and bone are composed of organized assemblies of carbonated apatite crystals, enamel is unusual in that it does not contain collagen nor does it remodel. Self-assembly of amelogenin protein into nanospheres has been recognized as a key factor in controlling the oriented and elongated growth of carbonated apatite crystals during dental enamel biomineralization. We report the in vitro formation of birefringent microribbon structures that were generated through the supramolecular assembly of amelogenin nanospheres. These microribbons have diffraction patterns that indicate a periodic structure of crystalline units along the long axis. The growth of apatite crystals orientated along the c axis and parallel to the long axes of the microribbons was observed in vitro. The linear arrays (chains) of nanospheres observed as intermediate states before the microribbon formation give an important indication as to the function of amelogenin in controlling the oriented growth of apatite crystals during enamel mineralization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Du, Chang -- Falini, Giuseppe -- Fermani, Simona -- Abbott, Christopher -- Moradian-Oldak, Janet -- R01 DE013414/DE/NIDCR NIH HHS/ -- R01-DE-13414/DE/NIDCR NIH HHS/ -- R21-DE-15332/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 2005 Mar 4;307(5714):1450-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Craniofacial Molecular Biology, School of Dentistry, University of Southern California, 2250 Alcazar Street, CSA 103, Los Angeles, CA 90033, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746422" target="_blank"〉PubMed〈/a〉
Keywords:
*Amelogenesis
;
Amelogenin
;
Animals
;
Birefringence
;
Crystallization
;
Dental Enamel Proteins/*chemistry/metabolism
;
Durapatite/chemistry
;
Hydrophobic and Hydrophilic Interactions
;
Microscopy, Atomic Force
;
Microscopy, Electron
;
*Nanotubes
;
Phosvitin
;
Protein Folding
;
Protein Structure, Quaternary
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Recombinant Proteins/chemistry
;
Swine
;
X-Ray Diffraction
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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