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

• Published in: Nature communications 2019-10, Vol.10 (1), p.4708-9, Article 4708
• Main Authors: Rho, Julia Y., Cox, Henry, Mansfield, Edward D. H., Ellacott, Sean H., Peltier, Raoul, Brendel, Johannes C., Hartlieb, Matthias, Waigh, Thomas A., Perrier, Sébastien
• Format: Article
• Language: English
• Subjects: 140/131; 147/143; 639/301/357/341; 639/301/357/354; 639/638/455/960; 639/638/541/966; Assembling; Cell Survival; Core loss; Dismantling; Humanities and Social Sciences; Humans; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Hydrophobicity; Macromolecular Substances - chemistry; multidisciplinary; Nanotechnology; Nanotubes; Nanotubes, Peptide - chemistry; PC-3 Cells; Peptides; Peptides - chemistry; Protein Conformation, beta-Strand; Science; Science (multidisciplinary); Self-assembly; Solubility; Thermodynamics; Water - chemistry
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-019-12586-8

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. Reversibility of peptide hydrogen bonded supramolecular assemblies makes them tunable but highly dynamic and prone to disassembly at the low concentration. Here the authors show a secondary hydrophobic interaction, near the peptide core that stabilises the peptide bonds, without losing the solubility of the systems in aqueous conditions.