Nanoscale Assembly of Functional Peptides with Divergent Programming Elements.
amyloid
chirality
d-amino acids
hydrogels
peptide
proline
self-assembly
Journal
ACS nano
ISSN: 1936-086X
Titre abrégé: ACS Nano
Pays: United States
ID NLM: 101313589
Informations de publication
Date de publication:
23 02 2021
23 02 2021
Historique:
pubmed:
13
2
2021
medline:
15
5
2021
entrez:
12
2
2021
Statut:
ppublish
Résumé
Self-assembling peptides are being applied both in the biomedical area and as building blocks in nanotechnology. Their applications are closely linked to their modes of self-assembly, which determine the functional nanostructures that they form. This work brings together two structural elements that direct nanoscale self-association in divergent directions: proline as a β-breaker and the β-structure-associated diphenylalanine motif, into a single tripeptide sequence. Amino acid chirality was found to resolve the tension inherent to these conflicting self-assembly instructions. Stereoconfiguration determined the ability of each of the eight possible Pro-Phe-Phe stereoisomers to self-associate into diverse nanostructures, including nanoparticles, nanotapes, or fibrils, which yielded hydrogels with gel-to-sol transition at a physiologically relevant temperature. Three single-crystal structures and all-atom molecular dynamics simulations elucidated the ability of each peptide to establish key interactions to form long-range assemblies (
Identifiants
pubmed: 33576622
doi: 10.1021/acsnano.0c09386
pmc: PMC8023796
doi:
Substances chimiques
Amyloid
0
Hydrogels
0
Peptides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3015-3025Références
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