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Enzymatic processing of amelogenin during continuous crystallization of apatite

  • Author(s): Uskoković, V
  • Kim, MK
  • Li, W
  • Habelitz, S
  • et al.

Published Web Location

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2631549/
No data is associated with this publication.
Abstract

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. © 2008 Materials Research Society.

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