期刊
NATURE COMMUNICATIONS
卷 9, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-07583-2
关键词
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资金
- National Natural Science Foundation of China [21673293, 21573287, 21425523]
- UK Engineering and Physical Science Research Council (EPSRC)
- Innovate UK [EP/F062966/1, KTP008143]
- NSF [DMR-0520547]
- European Union's Horizon 2020 research and innovation programme under the SINE2020 project [654000]
Peptide self-assembly is a hierarchical process, often starting with the formation of a-helices, beta-sheets or beta-hairpins. However, how the secondary structures undergo further assembly to form higher-order architectures remains largely unexplored. The polar zipper originally proposed by Perutz is formed between neighboring beta-strands of poly-glutamine via their side-chain hydrogen bonding and helps to stabilize the sheet. By rational design of short amphiphilic peptides and their self-assembly, here we demonstrate the formation of polar zippers between neighboring beta-sheets rather than between beta-strands within a sheet, which in turn intermesh the beta-sheets into wide and flat ribbons. Such a super-secondary structural template based on well-defined hydrogen bonds could offer an agile route for the construction of distinctive nanostructures and nanomaterials beyond beta-sheets.
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