Nanoribbons self-assembled from short peptides demonstrate the formation of polar zippers between β sheets

Meng Wang, Jiqian Wang, Peng Zhou, Jing Deng, Yurong Zhao, Yawei Sun, Yang Wei, Dong Wang, Zongyi Li, Xuzhi Hu, Stephen M. King, Sarah Rogers, Henry Cox, Thomas Waigh, Yang Jun, Jian Lu, Hai Xu

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Peptide self-assembly is a hierarchical process, often starting with the formation of α-helices, β-sheets or β-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 β-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 β-sheets rather than between β-strands within a sheet, which in turn intermesh the β-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 β-sheets.
    Original languageEnglish
    Article number5118
    JournalNature Communications
    Volume9
    Early online date30 Nov 2018
    DOIs
    Publication statusPublished - 2018

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