Ontology highlight
ABSTRACT:
SUBMITTER: Rho JY
PROVIDER: S-EPMC6797743 | biostudies-literature | 2019 Oct
REPOSITORIES: biostudies-literature
Rho Julia Y JY Cox Henry H Mansfield Edward D H EDH Ellacott Sean H SH Peltier Raoul R Brendel Johannes C JC Hartlieb Matthias M Waigh Thomas A TA Perrier Sébastien S
Nature communications 20191017 1
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 ...[more]