Enzymatic processing of amelogenin during continuous crystallization of apatite

Dental enamel forms through a protein-controlled mineralization and enzymatic degradation process with a nanoscale precision that new engineering technologies may be able to mimic. Recombinant full-length human amelogenin (rH174) and a matrix-metalloprotease (MMP-20) were used in a pH-stat titration...

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Bibliographic Details
Published in:Journal of materials research 2008-12, Vol.23 (12), p.3184-3195
Main Authors: Uskoković, V., Kim, M-K., Li, W., Habelitz, S.
Format: Article
Language:English
Subjects:
Applied and Technical Physics
Biomaterials
Biomimetic (assembly)
Ceramic
Inorganic Chemistry
Materials Engineering
Materials Science
Nanotechnology
Nucleation & growth
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Summary:Dental enamel forms through a protein-controlled mineralization and enzymatic degradation process with a nanoscale precision that new engineering technologies may be able to mimic. Recombinant full-length human amelogenin (rH174) and a matrix-metalloprotease (MMP-20) were used in a pH-stat titration system that enabled a continuous supply of calcium and phosphate ions over several days, mimicking the initial stages of matrix processing and crystallization in enamel in vitro. Effects on the self-assembly and crystal growth from a saturated aqueous solution containing 0.4 mg/mL rH174 and MMP-20 with the weight ratio of 1:1000 with respect to rH174 were investigated. A transition from nanospheres to fibrous amelogenin assemblies was facilitated under conditions that involved interaction between rH174 and its proteolytic cleavage products. Despite continuous titration, the levels of calcium exhibited a consistent trend of decreasing, thereby indicating a possible role in protein self-assembly. This study suggests that mimicking enamel formation in vitro requires the synergy between the aspects of matrix self-assembly, proteolysis, and crystallization.
ISSN:0884-2914
2044-5326
DOI:10.1557/JMR.2008.0387