Secondary Self-Assembly of Supramolecular Nanotubes into Tubisomes and Their Activity on Cells

Johannes C. Brendel, Joaquin Sanchis, Sylvain Catrouillet, Ewa Czuba, Moore Z. Chen, Benjamin M. Long, Cameron Nowell, Angus Johnston, Katrina A. Jolliffe, Sébastien Perrier

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41 Citations (Scopus)


The properties and structures of viruses are directly related to the three-dimensional structure of their capsid proteins, which arises from a combination of hydrophobic and supramolecular interactions, such as hydrogen bonds. The design of synthetic materials demonstrating similar synergistic interactions still remains a challenge. Herein, we report the synthesis of a polymer/cyclic peptide conjugate that combines the capability to form supramolecular nanotubes via hydrogen bonds with the properties of an amphiphilic block copolymer. The analysis of aqueous solutions by scattering and imaging techniques revealed a barrel-shaped alignment of single peptide nanotubes into a large tubisome (length: 260 nm (from SANS)) with a hydrophobic core (diameter: 16 nm) and a hydrophilic shell. These systems, which have a structure that is similar to those of viruses, were tested in vitro to elucidate their activity on cells. Remarkably, the rigid tubisomes are able to perforate the lysosomal membrane in cells and release a small molecule into the cytosol.

Original languageEnglish
Pages (from-to)16678-16682
Number of pages5
JournalAngewandte Chemie - International Edition
Issue number51
Publication statusPublished - 17 Dec 2018


  • cyclic peptides
  • lysosomal escape
  • nanotubes
  • supramolecular assemblies

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