Dual self-assembly of supramolecular peptide nanotubes to provide stabilisation in water.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 31624265.
- Also identified by DOI 10.1038/s41467-019-12586-8 and PMC identifier 6797743.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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 β-sheet hydrogen bonded architectures.
Medical subject headings
- Macromolecular Substances
- Nanotubes, Peptide
- Peptides
- Protein Conformation, beta-Strand
- Water