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Secondary Self‐Assembly of Supramolecular Nanotubes into Tubisomes and Their Activity on Cells
Author(s) -
Brendel Johannes C.,
Sanchis Joaquin,
Catrouillet Sylvain,
Czuba Ewa,
Chen Moore Z.,
Long Benjamin M.,
Nowell Cameron,
Johnston Angus,
Jolliffe Katrina A.,
Perrier Sébastien
Publication year - 2018
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201808543
Subject(s) - supramolecular chemistry , amphiphile , hydrogen bond , self assembly , supramolecular assembly , membrane , supramolecular polymers , chemistry , molecule , copolymer , macromolecule , peptide , capsid , polymer , biophysics , nanotechnology , materials science , organic chemistry , biochemistry , biology , gene
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.