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Modulation of Crystal Growth by the Terminal Sequences of the Prismatic-Associated Asprich Protein

机译：晶体生长的棱镜相关的Asprich蛋白的终端序列的调制。

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摘要

The formation of calcite in the mollusk shell prismatic layer requires the participation of various proteins. Recent studies indicate that the prismatic-associated protein superfamily, Asprich, is capable of in vitro stabilization of amorphous calcium carbonate (ACC), a precursor phase of prismatic calcite. To learn more about the molecular behavior of Asprich, we performed experiments on two highly conserved sequences derived from Asprich: Fragment-1, a 48 AA N-terminal cationic-anionic sequence, and Fragment-2, a previously characterized 42 C-terminal AA anionic sequence. SEM analyses reveal that Fragment-1 induces polycrystalline, radial aggregate assemblies of calcite, with evidence of surface porosities. AFM flow cell experiments demonstrate that Fragment-1 is multifunctional and its mineralization behavior is qualitatively similar to that reported for Fragment-2 except for hillock step kinetics. Surprisingly, when Fragment-1 and Fragment-2 are present together within the same assay, we observe phase stabilization of vaterite on Kevlar substrates and amorphous-appearing islands on calcite substrates. We believe that island formation on the calcite substrate results from the deposition of peptide-mineral clusters onto calcite hillock terrace surfaces. These events may also take place on the Kevlar substrate as well, where either vaterite or calcite form. The most significant feature is that a mixture of Fragment-1 + Fragment-2 are required to induce these effects and that the individual sequences themselves do not have this capability. These results indicate that these conserved terminal Asprich sequences jointly exhibit mineralization behavior (i.e., phase stabilization) that is qualitatively similar to the parent protein, and, parallels the in vitro findings reported for other calcite and aragonite - associated polypeptide sequences. It is likely that the sequence features of Asprich may be used to design crystal growth mimetics that can modulate crystal growth within the laboratory setting.
机译：软体动物壳棱形层中方解石的形成需要各种蛋白质的参与。最近的研究表明，棱柱形相关蛋白超家族Asprich能够在体外稳定无定形方解石的前体相无定形碳酸钙（ACC）。要了解有关Asprich分子行为的更多信息，我们对衍生自Asprich的两个高度保守的序列进行了实验：Fragment-1（一个48 AA N末端阳离子-阴离子序列）和Fragment-2（一个先前表征的42 C末端AA）阴离子序列。 SEM分析表明，Fragment-1诱导了方解石的多晶径向聚集体聚集，并显示出表面孔隙。 AFM流动池实验证明Fragment-1具有多功能性，除小丘阶跃动力学外，其矿化行为与Fragment-2报告的定性相似。令人惊讶的是，当片段1和片段2在同一测定中同时存在时，我们观察到凯夫拉尔基底上的球ate石和方解石基底上出现无定形的岛的相稳定。我们认为方解石基质上的岛形成是由于肽-矿物质簇沉积到方解石丘陵阶地表面上造成的。这些事件也可能发生在凯夫拉尔基质上，无论是球ate石还是方解石形式。最重要的特征是需要使用Fragment-1 + Fragment-2的混合物来诱导这些作用，并且各个序列本身不具备此功能。这些结果表明，这些保守的末端Asprich序列共同表现出矿化行为（即，相稳定），其在质量上与亲本蛋白质相似，并且与报道的与其他方解石和文石相关的多肽序列的体外发现相平行。 Asprich的序列特征可能会用于设计晶体生长模拟物，该模拟物可以在实验室环境中调节晶体生长。

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