Effects of Peptides on CaCO3 Crystallization : Mineralization Properties of an Acidic Peptide Isolated from Exoskeleton of Crayfish and Its Derivatives
Effects of Peptides on CaCO3 Crystallization : Mineralization Properties of an Acidic Peptide Isolated from Exoskeleton of Crayfish and Its Derivatives
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DOI：
10.1021/cg800447w
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发表时间：
2008-09
影响因子：
3.8
通讯作者：
Yuya Yamamoto;T. Nishimura;Ayae Sugawara;H. Inoue;H. Nagasawa;Takashi Kato
中科院分区：
文献类型：
--
作者：
Yuya Yamamoto;T. Nishimura;Ayae Sugawara;H. Inoue;H. Nagasawa;Takashi Kato
酸性蛋白质在生物矿化过程中起着关键作用。在此，我们报道了一种从小龙虾及其衍生物外骨骼中分离出来的酸性多肽--钙化相关肽-1(CAP-1)对碳酸钙在玻璃和甲壳素基质上结晶的影响。碳酸钙晶体的形态取决于多肽的化学结构。在甲壳素基质上，由于甲壳素结合区域的作用，形成了单轴取向的CaCO3晶体。结果表明，C端酸性区域和第70位磷酸丝氨酸对CaCO3结晶有较大影响。
Acidic proteins play key roles in biomineralization processes. Herein, we report on the effects of an acidic peptide, calcification associated peptide-1 (CAP-1), isolated from the exoskeleton of the crayfish and its derivatives on crystallization of CaCO3 on glass and chitin substrates. The morphologies of CaCO3 crystals depended on the chemical structure of the peptides. On chitin matrices, uniaxially oriented CaCO3 crystals were formed due to the effects of the specific chitin binding region of the peptides. It was revealed that the C-terminal acidic region and the 70th phosphoserine exerted great effects on CaCO3 crystallization.