Dual self-assembly of supramolecular peptide nanotubes to provide stabilisation in water.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
17 10 2019
17 10 2019
Historique:
received:
16
05
2019
accepted:
13
09
2019
entrez:
19
10
2019
pubmed:
19
10
2019
medline:
25
1
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 31624265
doi: 10.1038/s41467-019-12586-8
pii: 10.1038/s41467-019-12586-8
pmc: PMC6797743
doi:
Substances chimiques
Macromolecular Substances
0
Nanotubes, Peptide
0
Peptides
0
Water
059QF0KO0R
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4708Subventions
Organisme : Medical Research Council
Pays : United Kingdom
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