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

Abstract

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.1 The design of synthetic materials demonstrating similar synergistic interactions still remains a challenge.2 Here, we report the synthesis of a polymer/cyclic peptide conjugate, which 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: 250 nm) with a hydrophobic core (diameter: 16 nm) and a hydrophilic shell. These systems, which have a structure that is similar to a virus, were tested in‐vitro to elucidate their activity on cells. Remarkably, the rigid tubisomes demonstrated the ability to perforate the lysosomal membrane in cells and release a small molecule into the cytosol.