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Enzymatic processing of amelogenin during continuous crystallization of apatite

Published online by Cambridge University Press:  31 January 2011

V. Uskoković ,
M-K. Kim ,
W. Li  and
S. Habelitz
V. Uskoković*
Affiliation:
Division of Biomaterials and Bioengineering, Department of Preventive and Restorative Dental Sciences, University of California–San Francisco, San Francisco, California 94143
M-K. Kim
Affiliation:
Division of Biomaterials and Bioengineering, Department of Preventive and Restorative Dental Sciences, University of California–San Francisco, San Francisco, California 94143; and Department of Molecular and Cell Biology, University of California–Berkeley, Berkeley, California 94720-3200
W. Li
Affiliation:
Department of Oral and Craniofacial Sciences, University of California–San Francisco, San Francisco, California 94143
S. Habelitz
Affiliation:
Division of Biomaterials and Bioengineering, Department of Preventive and Restorative Dental Sciences, University of California–San Francisco, San Francisco, California 94143
*
a)Address all correspondence to this author. e-mail: vuk.uskokovic@ucsf.edu
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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.

Keywords

Biomimetic (assembly)CeramicNucleation & growth
Type
Articles
Information
Journal of Materials Research , Volume 23 , Issue 12: Biomimetic and Bio-enabled Materials Science and Engineering , December 2008 , pp. 3184 - 3195
Copyright
Copyright © Materials Research Society 2008

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