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Dual self-assembly of supramolecular peptide nanotubes to provide stabilisation in water.


ABSTRACT: Self-assembling peptides have the ability to spontaneously aggregate into large ordered structures. The reversibility of the peptide hydrogen bonded supramolecular assembly make them tunable to a host of different applications, although it leaves them highly dynamic and prone to disassembly at the low concentration needed for biological applications. Here we demonstrate that a secondary hydrophobic interaction, near the peptide core, can stabilise the highly dynamic peptide bonds, without losing the vital solubility of the systems in aqueous conditions. This hierarchical self-assembly process can be used to stabilise a range of different ?-sheet hydrogen bonded architectures.

PROVIDER: S-EPMC6797743 | BioStudies |

REPOSITORIES: biostudies

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