TY - JOUR
T1 - Dual self-assembly of supramolecular peptide nanotubes to provide stabilisation in water
AU - Rho, Julia Y.
AU - Cox, Henry
AU - Mansfield, Edward
AU - Ellacott, Sean H.
AU - Peltier, Raoul
AU - Brendel, Johannes C.
AU - Hartlieb, Matthias
AU - Waigh, Thomas
AU - Perrier, Sébastien
PY - 2019/10/17
Y1 - 2019/10/17
N2 - 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 β-sheet hydrogen bonded architectures.
AB - 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 β-sheet hydrogen bonded architectures.
UR - https://www.scopus.com/pages/publications/85073596297
U2 - 10.1038/s41467-019-12586-8
DO - 10.1038/s41467-019-12586-8
M3 - Article
SN - 2041-1723
VL - 10
JO - Nature Communications
JF - Nature Communications
M1 - 4708
ER -