Fibrillar amyloids exhibit a fascinating range of mechanical, optical, and electronic properties originating from their characteristic β-sheet-rich structure. Harnessing these functionalities in practical applications has so far been hampered by a limited ability to control the amyloid self-assembly process at the macroscopic scale. Here, we use core–shell electrospinning with microconfinement to assemble amyloid-hybrid fibers, consisting of densely aggregated fibrillar amyloids stabilized by a polymer shell. Up to centimeter-long hybrid fibers with micrometer diameter can be arranged into aligned and ordered arrays and deposited onto substrates or produced as free-standing networks. Properties that are characteristic of amyloids, including their high elastic moduli and intrinsic fluorescence signature, are retained in the hybrid fiber cores, and we show that they fully persist through the macroscopic fiber patterns. Our findings suggest that microlevel confinement is key for the guided assembly of amyloids from monomeric proteins.

中文翻译：

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长距离有序本征荧光淀粉样蛋白纤维的引导组装和构图

纤维状淀粉样蛋白表现出令人着迷的机械，光学和电子特性，这源于其特征性的富含β-折叠的结构。迄今为止，在实际应用中利用这些功能受到在宏观尺度上控制淀粉样蛋白自组装过程的有限能力的阻碍。在这里，我们使用具有微约束的核壳电纺组装淀粉样混合纤维，该纤维由通过聚合物壳稳定的密集聚集的纤维状淀粉样蛋白组成。可以将直径达1厘米的最长混合纤维排列成排列有序的阵列，然后沉积到基材上或制成独立式网络。淀粉样蛋白的特征，包括它们的高弹性模量和固有的荧光特征，保留在杂化纤维芯中，并且我们证明了它们在宏观纤维图案中完全存在。我们的研究结果表明，微级限制对于从单体蛋白中引导淀粉样蛋白的组装至关重要。