ArticleACS chemical neuroscience2024
Pore Formation by Amyloid-like Peptides: Effects of the Nonpolar-Polar Sequence Pattern.
Article in ACS chemical neuroscience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
The trial behind it
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Who cites it
3 citing papers in PubMed.
- Aggregation of Amyloid-like Peptides in Different Solvents.Journal of molecular liquids · 2026Article
- Interfacial Interactions of Nanoparticles and Molecular Nanostructures with Model Membrane Systems: Mechanisms, Methods, and Applications.Membranes · 2026Review
- Insights into Membrane Damage byBiomolecules · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
One of the mechanisms accounting for the toxicity of amyloid peptides in diseases like Alzheimer's and Parkinson's is the formation of pores on the plasma membrane of neurons. Here, we perform unbiased all-atom simulations of the full membrane damaging pathway, which includes adsorption, aggregation, and perforation of the lipid bilayer accounting for pore-like structures. Simulations are performed using four peptides made with the same amino acids. Differences in the nonpolar-polar sequence pattern of these peptides prompt them to adsorb into the membrane with the extended conformations oriented either parallel [peptide labeled F1, Ac-(FKFE)
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