ArticleBiophysics and physicobiology2025
Molecular dynamics simulations of amyloid-β(29-42) aggregation in bulk water and at the air-water interface.
Article in Biophysics and physicobiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed.
- A lattice Monte Carlo model for amyloid fibril formation.Biophysics and physicobiology · 2026Article
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3 authors.
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Abstract
Oligomers of amyloid-β (Aβ) peptides are related to Alzheimer's disease, and their formation is accelerated at hydrophilic-hydrophobic interfaces. We performed all-atom molecular dynamics simulations of Aβ(29-42) peptides in bulk water and at an air-water interface. In bulk water, the fragments formed stable aggregates, and the secondary structures were hardly changed. At the interface, the peptides were more easily separated from each other due to the low free-energy barrier and changed their secondary structures more frequently. This conformational flexibility is likely to promote amyloid fibril growth, suggesting a key role of interfacial environments in early aggregation processes.
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