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  • Title: Amelogenin supra-molecular assembly in vitro compared with the architecture of the forming enamel matrix.
    Author: Moradian-Oldak J, Goldberg M.
    Journal: Cells Tissues Organs; 2005; 181(3-4):202-18. PubMed ID: 16612086.
    Abstract:
    Tooth enamel is formed in the extracellular space within an organic matrix enriched in amelogenin proteins. Amelogenin nanosphere assembly is a key factor in controlling the oriented and organized growth of enamel apatite crystals. Recently, we have reported the formation of higher ordered structures resulting from organized association and self-orientation of amelogenin nanospheres in vitro. This remarkable hierarchical organization includes self-assembly of amelogenin molecules into subunits of 4-6 nm in diameter followed by their assembly to form nanospheres of 15-25 nm in radii. Chains of >100 nm length are then formed as the result of nanosphere association. These linear arrays of nanospheres assemble to form the microribbons that are hundreds of microns in length, tens of microns in width, and a few microns in thickness. Here, we review the step by step process of amelogenin self-assembly during the formation of microribbon structures in vitro. Assembly properties of selected amelogenins lacking the hydrophilic C terminus will then be reviewed. We will consider amelogenin as a template for the organized growth of crystals in vitro. Finally, we will compare the structures formed in vitro with globular and periodic structures observed earlier, in vivo, by different sample preparation conditions. We propose that the alignment of amelogenin nanospheres into long chains is evident in vivo, and is an important indication for the function of this protein in controlling the oriented and elongated growth of apatite crystals during enamel biomineralization.
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