Biophysical characterization as a tool to predict amyloidogenic and toxic properties of amyloid-β42 peptides.
Alzheimer disease
amyloid toxicity
amyloid-β peptides
amyloidogenicity
bioactivity
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
06 2022
06 2022
Historique:
revised:
02
04
2022
received:
02
02
2022
accepted:
19
04
2022
pubmed:
26
4
2022
medline:
16
6
2022
entrez:
25
4
2022
Statut:
ppublish
Résumé
Amyloid-β42 (Aβ42) peptides are central to the amyloid pathology in Alzheimer's disease (AD). As biological mimetics, properties of synthetic Aβ peptides usually vary between vendors and batches, thus impacting the reproducibility of experimental studies. Here, we tested recombinantly expressed Aβ42 (Asp1 to Ala42) against synthetic Aβ42 from different suppliers using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), circular dichroism (CD) spectroscopy, thioflavin T aggregation, surface plasmon resonance, and MTT cell viability assays. Overall, our recombinant Aβ42 provided a reproducible mimetic of desired properties. Across experimental approaches, the combined detection of Aβ42 dimers and random coil to β-sheet transition only correlated with aggregation-prone and cytotoxic peptides. Conclusively, combining MALDI-MS with CD appears to provide a rapid, reliable means to predict the 'bioactivity' of Aβ42.
Identifiants
pubmed: 35466397
doi: 10.1002/1873-3468.14358
doi:
Substances chimiques
Amyloid beta-Peptides
0
Peptide Fragments
0
amyloid beta-protein (1-42)
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1401-1411Subventions
Organisme : CIHR
Pays : Canada
Informations de copyright
© 2022 Federation of European Biochemical Societies.
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