Abstract

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.

Full Text
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