In vitro regulation of CaCO3 crystal polymorphism by the highly acidic molluscan shell protein Aspein
In vitro regulation of CaCO3 crystal polymorphism by the highly acidic molluscan shell protein Aspein
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DOI：
10.1016/j.febslet.2008.01.026
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发表时间：
2008-03
期刊：
影响因子：
3.5
通讯作者：
Takeshi Takeuchi;I. Sarashina;M. Iijima;K. Endo
中科院分区：
文献类型：
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作者：
Takeshi Takeuchi;I. Sarashina;M. Iijima;K. Endo
生物矿物质，尤其是软体动物的壳，通常含有异常酸性的蛋白质。这些蛋白质被认为在晶体成核和抑制中起作用。我们之前从珍珠贝 Pinctada fucata 中发现了一种异常酸性的蛋白质 Aspein。在这里，我们证明 Aspein 可以在体外控制 CaCO3 多晶型物（方解石/文石）。虽然文石优先在富含 Mg2+ 的溶液中形成，模仿海洋软体动物的外液，但 Aspein 专门诱导方解石沉淀。我们的结果表明，Aspein 参与了棱柱层中特定方解石的形成。使用截短的 Aspein 进行的实验表明，富含天冬氨酸的结构域对于方解石沉淀至关重要。
Biominerals, especially molluscan shells, generally contain unusually acidic proteins. These proteins are believed to function in crystal nucleation and inhibition. We previously identified an unusually acidic protein Aspein from the pearl oyster Pinctada fucata. Here we show that Aspein can control the CaCO3polymorph (calcite/aragonite) in vitro. While aragonite is preferentially formed in Mg2+-rich solutions imitating the extrapallial fluids of marine molluscs, Aspein exclusively induced calcite precipitation. Our results suggest that Aspein is involved in the specific calcite formation in the prismatic layer. Experiments using truncated Aspein demonstrated that the aspartic acid rich domain is crucial for the calcite precipitation.