ArticleChemphyschem : a European journal of chemical physics and physical chemistry2021
Early Divergence in Misfolding Pathways of Amyloid-Beta Peptides.
Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- From Disordered to Ordered: Nanoscale Spectroscopy Reveals Structural Evolution of Amyloid Beta 40 Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Biophysical insights into the molecular mechanisms of beta amyloid aggregation and its toxic effects in Alzheimer's disease.Frontiers in molecular biosciences · 2025Review
- Large dynamics of a phase separating arginine-glycine-rich domain revealed via nuclear and electron spins.Nature communications · 2024Article
- Early stages of misfolding of PAP248-286 at two different pH values: An insight from molecular dynamics simulations.Computational and structural biotechnology journal · 2022Article
- Early Divergence in Misfolding Pathways of Amyloid-Beta Peptides.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021Article
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Authors and funding
4 authors.
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Abstract
The amyloid cascade hypothesis proposes that amyloid-beta (Aβ) aggregation is the initial triggering event in Alzheimer's disease. Here, we utilize NMR spectroscopy and monitor the structural dynamics of two variants of Aβ, Aβ40 and Aβ42, as a function of temperature. Despite having identical amino acid sequence except for the two additional C-terminal residues, Aβ42 has higher aggregation propensity than Aβ40. As revealed by the NMR data on dynamics, including backbone chemical shifts, intra-methyl cross-correlated relaxation rates and glycine-based singlet-states, the C-terminal region of Aβ, especially the G33-L34-M35 segment, plays a particular role in the early steps of temperature-induced Aβ aggregation. In Aβ42, the distinct dynamical behaviour of C-terminal residues at higher temperatures is accompanied with marked changes in the backbone dynamics of residues V24-K28. The distinctive role of the C-terminal region of Aβ42 in the initiation of aggregation defines a target for the rational design of Aβ42 aggregation inhibitors.
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Registered trials
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