Silica Nanowires Templated by Amyloid-like Fibrils.
Silica Nanowires Templated by Amyloid-like Fibrils.
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DOI：
10.1002/ange.201508415
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发表时间：
2015-11-02
期刊：
影响因子：
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通讯作者：
Serpell LC
中科院分区：
文献类型：
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作者：
Al-Garawi ZS;Thorpe JR;Serpell LC
许多肽自组装形成淀粉样纤维。我们先前使用具有序列KFFEAAAKKFFE的设计肽的变体探索了形成淀粉样蛋白的序列倾向。这些变体肽形成具有不同侧向组装的高度稳定的淀粉样蛋白原纤维，并且是理想的非蛋白质材料的进一步组装的模板。在本文中，我们表明由肽变体形成的原纤维可以用二氧化硅层涂覆以使用原硅酸四乙酯产生二氧化硅纳米线。使用电子显微镜（TEM）、X射线纤维衍射、FTIR和横截面EM表征所得纳米线以揭示具有肽核心的纳米结构。赖氨酸残基发挥的作用，在模板上的纤维表面上的二氧化硅的形成，并使用这个库的肽，我们已经探讨了贡献的赖氨酸以及精氨酸的二氧化硅模板，并发现序列起着重要的作用，在确定的物理性质和结构的所得纳米线。
Many peptides self‐assemble to form amyloid fibrils. We previously explored the sequence propensity to form amyloid using variants of a designed peptide with sequence KFFEAAAKKFFE. These variant peptides form highly stable amyloid fibrils with varied lateral assembly and are ideal to template further assembly of non‐proteinaceous material. Herein, we show that the fibrils formed by peptide variants can be coated with a layer of silica to produce silica nanowires using tetraethyl‐orthosilicate. The resulting nanowires were characterized using electron microscopy (TEM), X‐ray fiber diffraction, FTIR and cross‐section EM to reveal a nanostructure with peptidic core. Lysine residues play a role in templating the formation of silica on the fibril surface and, using this library of peptides, we have explored the contributions of lysine as well as arginine to silica templating, and find that sequence plays an important role in determining the physical nature and structure of the resulting nanowires.