Secondary Self-Assembly of Supramolecular Nanotubes into Tubisomes and Their Activity on Cells.
Angew Chem Int Ed Engl
; 57(51): 16678-16682, 2018 12 17.
Article
in En
| MEDLINE
| ID: mdl-30383920
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. 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 260â
nm (from SANS)) with a hydrophobic core (diameter 16â
nm) and a hydrophilic shell. These systems, which have a structure that is similar to those of viruses, were tested inâ
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptides, Cyclic
/
Polymers
/
Nanotubes
Limits:
Humans
Language:
En
Journal:
Angew Chem Int Ed Engl
Year:
2018
Type:
Article
Affiliation country:
United kingdom