The design and assembly of peptide based materials has advanced considerably, leading to a variety of fibrous, sheet and nanoparticle structures. A remaining challenge is to account for and control different possible supramolecular outcomes accessible to the same or similar peptide building blocks. Here we present a de novo peptide system that forms nanoparticles or sheets depending on the strategic placement of a disulfide pin between two elements of secondary structure that drive self-assembly. Specifically, we join homodimerizing and homotrimerizing de novo coiled-coil α-helices with a flexible linker to generate a series of linear peptides. The helices are pinned back-to-back, constraining them as hairpins by a disulfide bond placed either proximal or distal to the linker. Computational modeling and advanced microscopy show that the proximally pinned hairpins self-assemble into nanoparticles, whereas the distally pinned constructs form sheets. These peptides can be made synthetically or recombinantly to allow both chemical modifications and the introduction of whole protein cargoes as required.

中文翻译：

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De Novo设计的肽和蛋白质发夹可自动组装成薄片和纳米颗粒。

肽基材料的设计和组装已经取得了很大进展，从而导致了各种纤维状，片状和纳米粒子结构。剩下的挑战是要解释和控制相同或相似的肽构建基块可能获得的不同的超分子结果。在这里，我们介绍了一种从头肽系统，该系统根据二硫键在驱动自组装的二级结构的两个元素之间的战略位置而形成纳米颗粒或薄片。具体来说，我们从头开始进行均二聚和均三聚带有柔性接头的卷曲螺旋α螺旋，可产生一系列线性肽。螺旋被背对背固定，通过置于连接子近端或远端的二硫键将它们限制为发夹。计算模型和高级显微镜显示，近端固定的发夹会自组装成纳米粒子，而远端固定的结构会形成薄片。这些肽可以合成或重组制备，以允许根据需要进行化学修饰和引入全蛋白货物。