Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 60, Issue 4, Pages 2099-2103Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202012470
Keywords
amyloid fibers; chirality; co-assembly; dipeptides; supramolecular gels
Categories
Funding
- National Natural Science Foundation of China [21961142022]
- China Postdoctoral Science Foundation [BX20190333, 2019M660804]
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This study successfully obtained supramolecular gels with a transition from amyloid-like beta-sheet to different supramolecular helices through co-assembly of a specific core recognition motif, revealing the vital roles of the microenvironment of chiral carbon and different stacking modes of additives in the chiral transfer or amplification of L-FmocFF. The dynamic process of helix formation was captured, providing a convenient co-assembly method to explore the structure basis of A beta fibrils with controlled chirality.
It is commonly considered that amyloid-beta (A beta) fibrils are heavily involved in the neurological diseases. Establishing an external model based on the core recognition motif (diphenylalanine, FF) of A beta would be of significance in understanding the assembly and disassembly of A beta fibrils in living system. Herein, supramolecular gels with structure transition from amyloid-like beta-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 A beta fibrils with a controlled chirality.
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