期刊
COMMUNICATIONS CHEMISTRY
卷 2, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s42004-019-0170-z
关键词
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资金
- European Research Council under the European Union Horizon 2020 research and innovation program [694426]
- National Natural Science Foundation of China [21522307, 21802143]
- National Natural Science Fund BRICS STI Framework Programme [51861145304]
- Innovation Research Community Science Fund [21821005]
- Key Research Program of Frontier Sciences of Chinese Academy of Sciences (CAS) [QYZDB-SSW-JSC034]
Conformational transitions of secondary structures are a crucial factor in many protein misfolding diseases. However, the actual transition of folded proteins into beta-sheet-rich structures is not fully understood. Inhibition of aggregate formation, mediated by the beta-sheet conformation, and control of the secondary structural transition of proteins and peptides could potentially attenuate the development of amyloid-associated diseases. Here we describe a stoichiometry-controlled secondary structure transition of amyloid-derived dipeptide assemblies from a beta-sheet to supramolecular helix conformation through coassembly with a bipyridine derivative. The transition is mainly mediated by the intermolecular hydrogen bonds and pi-pi interactions between the two components, which induce the altered stacking and conformation of the co-assemblies, as confirmed by experimental results and computational simulations. This work not only exemplifies a feasible strategy to disrupt the beta-sheet conformation, underlying amyloid-like fibril formation, but also provides a conceptual basis for the future utilization of the helical nanostructures in various biological applications.
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