ArticleLangmuir : the ACS journal of surfaces and colloids2014
Effects of polyamino acids and polyelectrolytes on amyloid β fibril formation.
Article in Langmuir : the ACS journal of surfaces and colloids, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Strategic physicochemical tuning: amphiphilic polymers as molecular regulators of amyloid aggregation and cytotoxicity.Chemical science · 2026Article
- Lysozyme Amyloid for Synthetic RNA Delivery.Pharmaceutics · 2025Article
- Fibrillization Process of Human Amyloid-Beta Protein (1-40) under a Molecular Crowding Environment Mimicking the Interior of Living Cells Using Cell Debris.Molecules (Basel, Switzerland) · 2023Article
- Controlling amyloid formation of intrinsically disordered proteins and peptides: slowing down or speeding up?Essays in biochemistry · 2022Article
- Real-Time Fast Amyloid Seeding and Translocation of α-Synuclein with a Nanopipette.ACS central science · 2022Article
- Nanomedicines in the Management of Alzheimer's Disease: Current View and Future Prospects.Frontiers in aging neuroscience · 2022Review
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Use of Biodegradable, Chitosan-Based Nanoparticles in the Treatment of Alzheimer's Disease.Molecules (Basel, Switzerland) · 2020Review
- A cationic polymethacrylate-copolymer acts as an agonist for β-amyloid and an antagonist for amylin fibrillation.Chemical science · 2019Article
- Trodusquemine enhances AβNature communications · 2019Article
- Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Chemical Society reviews · 2017Review
- Article
- Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones.Scientific reports · 2016Article
- Fluorescent filter-trap assay for amyloid fibril formation kinetics in complex solutions.ACS chemical neuroscience · 2015Article
- The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation.Chemical science · 2015Article
- On the lag phase in amyloid fibril formation.Physical chemistry chemical physics : PCCP · 2015Review
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Authors and funding
3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The fibril formation of the neurodegenerative peptide amyloid β (Aβ42) is sensitive to solution conditions, and several proteins and peptides have been found to retard the process. Aβ42 fibril formation was followed with ThT fluorescence in the presence of polyamino acids (poly-glutamic acid, poly-lysine, and poly-threonine) and other polymers (poly(acrylic acid), poly(ethylenimine), and poly(diallyldimethylammonium chloride). An accelerating effect on the Aβ42 aggregation process is observed from all positively charged polymers, while no effect is seen from the negative or neutral polymers. The accelerating effect is dependent on the concentration of positive polymer in a highly reproducible manner. Acceleration is observed from a 1:500 polymer to Aβ42 weight ratio and up. Polyamino acids and the other polymers exert quantitatively the same effect at the same concentrations based on weight. Fibrils are formed in all cases as verified by transmission electron microscopy. The concentrations of polymers required for acceleration are too low to affect the Aβ42 aggregation process through increased ionic strength or molecular crowding effects. Instead, the acceleration seems to arise from the locally increased Aβ42 concentration near the polymers, which favors association and affects the electrostatic environment of the peptide.
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