Acidic pH Promotes Refolding and Macroscopic Assembly of Amyloid β (16-22) Peptides at the Air-Water Interface.
Journal
The journal of physical chemistry letters
ISSN: 1948-7185
Titre abrégé: J Phys Chem Lett
Pays: United States
ID NLM: 101526034
Informations de publication
Date de publication:
28 Jul 2022
28 Jul 2022
Historique:
pubmed:
16
7
2022
medline:
30
7
2022
entrez:
15
7
2022
Statut:
ppublish
Résumé
Assembly by amyloid-beta (Aβ) peptides is vital for various neurodegenerative diseases. The process can be accelerated by hydrophobic interfaces such as the cell membrane interface and the air-water interface. Elucidating the assembly mechanism for Aβ peptides at hydrophobic interface requires knowledge of the microscopic structure of interfacial peptides. Here we combine scanning force microscopy, sum-frequency generation spectroscopy, and metadynamics simulations to probe the structure of the central fragment of Aβ peptides at the air-water interface. We find that the structure of interfacial peptides depends on pH: at neutral pH, the peptides adopt a less folded, bending motif by forming intra-hydrogen bonds; at acidic pH, the peptides refold into extended β-strand fibril conformation, which further promotes their macroscopic assembly. The conformational transition of interfacial peptides is driven by the reduced hydrogen bonds, both with water and within peptides, resulting from the protonation of acidic glutamic acid side chains.
Identifiants
pubmed: 35839425
doi: 10.1021/acs.jpclett.2c01171
pmc: PMC9340808
doi:
Substances chimiques
Amyloid
0
Amyloid beta-Peptides
0
Peptide Fragments
0
Water
059QF0KO0R
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
6674-6679Références
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