New cylindrical peptide assemblies defined by extended parallel β-sheets

Org Biomol Chem. 2013 Jan 21;11(3):425-9. doi: 10.1039/c2ob26637g. Epub 2012 Oct 9.

Abstract

A new approach to non-covalent peptide-based nanotubular or rod-like structures is presented, whereby the monomeric units are preorganised into a β-strand geometry that templates the formation of an extended and unusual parallel β-sheet rod-like structure. The conformational constraint is introduced by Huisgen cycloaddition to give a triazole-based macrocycle, with the resulting self-assembled structures stabilized by a well-defined series of intermolecular hydrogen bonds.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Models, Molecular
  • Oligopeptides / chemical synthesis*
  • Oligopeptides / chemistry
  • Protein Structure, Secondary

Substances

  • Oligopeptides