Peptides display a range of important properties, controlled by the intrinsic nature of organic side chains, regarding redox activity, charge density, and structure. Here, we demonstrate a new synthetic approach to insert non-coded amino acids that contain metal oxide groups into a desired peptide sequence with a commercial peptide synthesizer. This approach allowed us to design and isolate a range of highly anionic peptides with various sequences, including the amyloid Aβ_17–20, the amphiphilic KFE8, and a bacterial chaperone DnaK substrate. By taking advantage of both the inorganic polyoxometalate-based motif and the peptide sequence, the resultant POM peptides enable significant inhibition of amyloid aggregation, switch a β sheet into a β turn, and enhance binding with the molecular chaperone DnaK. Therefore, we show it is possible to program the robotic synthesis of peptides with functional inorganic amino acids as a generic approach for the design and exploration of next-generation artificial biological-inorganic structures.

肽显示出一系列重要的特性，这些特性受有机侧链的固有性质控制，涉及氧化还原活性、电荷密度和结构。在这里，我们展示了一种新的合成方法，使用商业肽合成仪将含有金属氧化物基团的非编码氨基酸插入所需的肽序列中。这种方法使我们能够设计和分离一系列具有不同序列的高阴离子肽，包括淀粉样蛋白 A β _17-20、两亲性 KFE8 和细菌伴侣 DnaK 底物。通过利用基于无机多金属氧酸盐的基序和肽序列，所得的 POM 肽能够显着抑制淀粉样蛋白的聚集，将 β 折叠转变为 β 转角，并增强与分子伴侣 DnaK 的结合。因此，我们展示了将具有功能性无机氨基酸的肽的机器人合成编程为设计和探索下一代人工生物-无机结构的通用方法是可能的。