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

Research output: Contribution to journalArticle

  • External authors:
  • 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
  • Yang Jun
  • Hai Xu

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.

Bibliographical metadata

Original languageEnglish
Article number5118
JournalNature Communications
Volume9
Early online date30 Nov 2018
DOIs
Publication statusPublished - 2018

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