Amelogenin supra-molecular assembly in vitro compared with the architecture of the forming enamel matrix
Amelogenin supra-molecular assembly in vitro compared with the architecture of the forming enamel matrix
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DOI：
10.1159/000091382
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发表时间：
2005-01-01
影响因子：
2.7
通讯作者：
Goldberg, M
中科院分区：
文献类型：
--
作者：
Moradian-Oldak, J;Goldberg, M
牙釉质形成于富含釉原蛋白的有机基质内的细胞外间隙中。釉原蛋白纳米球的组装是控制釉质磷灰石晶体定向有序生长的关键因素。最近，我们报道了釉原蛋白纳米球在体外形成的有序结构的有组织的协会和自我定位。这种显著的分级组织包括釉原蛋白分子自组装成直径为4-6 nm的亚基，然后组装形成半径为15-25 nm的纳米球。然后作为纳米球缔合的结果形成> 100 nm长度的链。这些纳米球的线性阵列组装形成长度为数百微米、宽度为数十微米、厚度为几微米的微带。本文综述了釉原蛋白在体外自组装形成微支架结构的过程。选择缺乏亲水性C末端的釉原蛋白的组装特性，然后将进行审查。我们将考虑将釉原蛋白作为体外晶体有序生长的模板。最后，我们将通过不同的样品制备条件，将体外形成的结构与早期在体内观察到的球状和周期性结构进行比较。我们建议，成釉蛋白纳米球的排列成长链在体内是显而易见的，并且是这种蛋白质在控制牙釉质生物矿化过程中磷灰石晶体的定向和伸长生长的功能的重要指示。版权所有（c）2005 S. Karger AG，巴塞尔。
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. Copyright (c) 2005 S. Karger AG, Basel.