| Literature DB >> 33048413 |
Aoli Wu1, Yongxian Guo1,2, Xianbao Li1,2, Huimin Xue1,2, Jinbo Fei1, Junbai Li1,2.
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.Entities:
Keywords: amyloid fibers; chirality; co-assembly; dipeptides; supramolecular gels
Year: 2020 PMID: 33048413 DOI: 10.1002/anie.202012470
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336