STRUCTURAL BIOLOGY OF THE ENAMEL PROTEINS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. The major goal of our research activities is to advance our understanding of the fundamental molecular mechanisms involved in the formation of dental enamel. We postulate that such understanding will lead to the future development of biomimetic strategies for the creation of enamel-like mineral materials. We focus on two areas: 1. The structure and function of enamel extracellular matrix components. 2) The function and mechanism of action of enamel proteinases MMP-20 and KLK-4. Our goals are: ( project #1) to identify the nature of the interactions which define protein self-assembly in solution and the nanosphere matrix architecture, at the molecular level, to define at the molecular level the ultrastructural architecture of amelogenin-based matrices formed in vitro, to characterize apatite and octacalcium phosphate crystal growth, morphology and orientation within synthetic amelogenin gel matrices in the absence and presence of the non-amelogenins. (project # 2) : To investigate the function of MMP-20 in the assembly, dis-assembly and apatite binding of amelogenin and its proteolytic products.