The prebiotic replication of information-coding molecules is a central problem concerning life's origins. Here, we report that amyloids composed of short peptides can direct the sequence-selective, regioselective and stereoselective condensation of amino acids. The addition of activated DL-arginine and DL-phenylalanine to the peptide RFRFR-NH₂ in the presence of the complementary template peptide Ac-FEFEFEFE-NH₂ yields the isotactic product FRFRFRFR-NH₂, 1 of 64 possible triple addition products, under conditions in which the absence of template yields only single and double additions of mixed stereochemistry. The templating mechanism appears to be general in that a different amyloid formed by (Orn)V(Orn)V(Orn)V(Orn)V-NH₂ and Ac-VDVDVDVDV-NH₂ is regioselective and stereoselective for N-terminal, L-amino-acid addition while the ornithine-valine peptide alone yields predominantly sidechain condensation products with little stereoselectivity. Furthermore, the templating reaction is stable over a wide range of pH (5.6-8.6), salt concentration (0-4 M NaCl), and temperature (25-90 °C), making the amyloid an attractive model for a prebiotic peptide replicating system.

中文翻译：

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基于淀粉样蛋白的益生元模板指导的肽合成。

信息编码分子的益生元复制是有关生命起源的主要问题。在这里，我们报道由短肽组成的淀粉样蛋白可以指导氨基酸的序列选择性，区域选择性和立体选择性缩合。在互补模板肽Ac-FEFEFEFE-NH ₂存在下，向肽RFRFR-NH ₂中添加活化的DL-精氨酸和DL-苯丙氨酸会产生等规产物FRFRFRFR-NH ₂，在64种可能的三重加成产物中在没有模板的情况下，只会产生一次和两次添加的混合立体化学反应。模板机制似乎是通用的，因为由（Orn）V（Orn）V（Orn）V（Orn）V-NH ₂形成的淀粉样蛋白不同Ac-VDVDVDVDV-NH ₂对N端L-氨基酸的添加具有区域选择性和立体选择性，而单独的鸟氨酸-缬氨酸肽主要产生侧链缩合产物，几乎没有立体选择性。此外，模板反应在广泛的pH（5.6-8.6），盐浓度（0-4 M NaCl）和温度（25-90°C）范围内都是稳定的，从而使淀粉样蛋白成为益生元肽复制的诱人模型系统。