It is commonly considered that amyloid‐β (Aβ) fibrils are heavily involved in the neurological diseases. Establishing an external model based on the core recognition motif (diphenylalanine, FF) of Aβ would be of significance in understanding the assembly and disassembly of Aβ fibrils in living system. Herein, supramolecular gels with structure transition from amyloid‐like β‐sheet to different supramolecular helices were obtained through the co‐assembly of a N‐fluorenylmethoxycarbonyl‐protected L‐FF (L‐FmocFF) with achiral pyridine derivatives. It is found that the different stacking modes (H‐ or J‐aggregates) of additives and the microenvironment of chiral carbon play vital roles for the selectively chiral transfer or amplification of L‐FmocFF. The dynamic process of helix formation was also captured. This work provides a convenient co‐assembly way to explore the structure basis of Aβ fibrils with a controlled chirality.

中文翻译：

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具有受控手性的二肽和吡啶衍生物的超分子凝胶共组装

通常认为淀粉样β（Aβ）原纤维大量参与神经系统疾病。建立基于Aβ核心识别基序（diphenylalanine，FF）的外部模型对于理解生命系统中Aβ原纤维的组装和拆卸具有重要意义。在此，通过N-芴基甲氧基羰基保护的L-FF（L-FmocFF）与非手性吡啶衍生物的共组装，获得了结构从淀粉样β-折叠转变为不同的超分子螺旋的超分子凝胶。发现添加剂的不同堆积模式（H-或J-聚集体）和手性碳的微环境对于L-FmocFF的选择性手性转移或扩增起着至关重要的作用。还捕获了螺旋形成的动态过程。