ArticleInternational journal of molecular sciences2020
The Clustering of mApoE Anti-Amyloidogenic Peptide on Nanoparticle Surface Does Not Alter Its Performance in Controlling Beta-Amyloid Aggregation.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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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Who cites it
4 citing papers in PubMed.
- Polyphenol-Rich Cinnamon Bud Extract Affects Ataxin-3 Aggregation and Ameliorates SCA3 Phenotypes Through a Dual Anti-Amyloidogenic and Antioxidant Mechanism.Molecules (Basel, Switzerland) · 2026Article
- Cell Membrane Biomimetic Nanoparticles with Potential in Treatment of Alzheimer's Disease.Molecules (Basel, Switzerland) · 2023Review
- Clinical progress of nanomedicine-based RNA therapies.Bioactive materials · 2022Review
- Strategies to deliver RNA by nanoparticles for therapeutic potential.Molecular aspects of medicine · 2022Review
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Authors and funding
13 authors.
Funding
Abstract
The deposition of amyloid-β (Aβ) plaques in the brain is a significant pathological signature of Alzheimer's disease, correlating with synaptic dysfunction and neurodegeneration. Several compounds, peptides, or drugs have been designed to redirect or stop Aβ aggregation. Among them, the trideca-peptide CWG-LRKLRKRLLR (mApoE), which is derived from the receptor binding sequence of apolipoprotein E, is effectively able to inhibit Aβ aggregation and to promote fibril disaggregation. Taking advantage of Atomic Force Microscopy (AFM) imaging and fluorescence techniques, we investigate if the clustering of mApoE on gold nanoparticles (AuNP) surface may affect its performance in controlling Aβ aggregation/disaggregation processes. The results showed that the ability of free mApoE to destroy preformed Aβ fibrils or to hinder the Aβ aggregation process is preserved after its clustering on AuNP. This allows the possibility to design multifunctional drug delivery systems with clustering of anti-amyloidogenic molecules on any NP surface without affecting their performance in controlling Aβ aggregation processes.
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