Non-Equilibrium Polymerization of Cross-β Amyloid Peptides for Temporal Control of Electronic Properties.
aggregation
gels
peptides
polymerization
self-assembly
Journal
Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543
Informations de publication
Date de publication:
03 08 2020
03 08 2020
Historique:
received:
12
03
2020
revised:
13
04
2020
pubmed:
30
4
2020
medline:
27
4
2021
entrez:
30
4
2020
Statut:
ppublish
Résumé
Hydrophobic collapse plays crucial roles in protein functions, from accessing the complex three-dimensional structures of native enzymes to the dynamic polymerization of non-equilibrium microtubules. However, hydrophobic collapse can also lead to the thermodynamically downhill aggregation of aberrant proteins, which has interestingly led to the development of a unique class of soft nanomaterials. There remain critical gaps in the understanding of the mechanisms of how hydrophobic collapse can regulate such aggregation. Demonstrated herein is a methodology for non-equilibrium amyloid polymerization through mutations of the core sequence of Aβ peptides by a thermodynamically activated moiety. An out of equilibrium state is realized because of the negative feedback from the transiently formed cross-β amyloid networks. Such non-equilibrium amyloid nanostructures were utilized to access temporal control over its electronic properties.
Identifiants
pubmed: 32348633
doi: 10.1002/anie.202003721
doi:
Substances chimiques
Amyloid beta-Peptides
0
Peptide Fragments
0
amyloid beta-protein (1-42)
0
Histidine
4QD397987E
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
13506-13510Informations de copyright
© 2020 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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