Calcium-Induced Molecular Rearrangement of Peptide Folds Enables Biomineralization of Vaterite Calcium Carbonate
Calcium-Induced Molecular Rearrangement of Peptide Folds Enables Biomineralization of Vaterite Calcium Carbonate
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DOI：
10.1021/jacs.8b00281
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发表时间：
2018-02-28
影响因子：
15
通讯作者：
Weidner, Tobias
中科院分区：
文献类型：
--
作者：
Lu, Hao;Lutz, Helmut;Weidner, Tobias
蛋白质可以通过选择性地触发方解石、文石或球文石相的生长来控制碳酸钙的矿化。蛋白质对CaCO 3的模板作用必须主要发生在蛋白质/CaCO 3界面上，但在活性矿化过程中缺乏对界面的分子水平的了解。在这里，我们调查的作用肽折叠和结构的灵活性上的矿化碳酸钙。我们研究了两个基于谷氨酸和亮氨酸的两亲性肽，具有β-折叠和α-螺旋结构。虽然两种序列都导致球文石结构，但β-片层产生具有上级稳定性和纯度的独立式球文石纳米片层。表面光谱和分子动力学模拟表明，钙离子和肽的相互结构导致通过模仿（001）晶面有效合成球文石。
Proteins can control mineralization of CaCO3 by selectively triggering the growth of calcite, aragonite or vaterite phases. The templating of CaCO3 by proteins must occur predominantly at the protein/CaCO3 interface, yet molecular-level insights into the interface during active mineralization have been lacking. Here, we investigate the role of peptide folding and structural flexibility on the mineralization of CaCO3. We study two amphiphilic peptides based on glutamic acid and leucine with beta-sheet and alpha-helical structures. Though both sequences lead to vaterite structures, the beta-sheets yield free-standing vaterite nanosheet with superior stability and purity. Surface-spectroscopy and molecular dynamics simulations reveal that reciprocal structuring of calcium ions and peptides lead to the effective synthesis of vaterite by mimicry of the (001) crystal plane.