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Dental enamel forms through a protein-controlled mineralization and enzymatic degradation with a nanoscale precision that new engineering technologies may be able to mimic. Recombinant fulllength human amelogenin (rH174) and a matrix-metalloprotease (MMP-20) were employed in a pHstat 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 an interaction between rH174 and the proteolytic cleavage products. Despite continuous titration, the levels of calcium exhibited a consistent trend of decreasing, thereby indicating its possible role in the 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.


This is a pre-copy-editing, author-produced PDF of an article accepted for publication in Journal of Materials Research, volume 23, issue 12, in 2008 following peer review. The definitive publisher-authenticated version is available online at DOI: 10.1557/JMR.2008.0387.


Cambridge University Press



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