ArticleInternational journal of molecular sciences2018
Exploring the Mechanism of Inhibition of Au Nanoparticles on the Aggregation of Amyloid-β(16-22) Peptides at the Atom Level by All-Atom Molecular Dynamics.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Nanotechnology to Overcome Blood-Brain Barrier Permeability and Damage in Neurodegenerative Diseases.Pharmaceutics · 2025Review
- Advance Nanotechnology-Based Drug Delivery Systems for Alzheimer's Disease: Advancements and Future Perspectives.Current Alzheimer research · 2025Review
- Changes in the Secondary Structure and Assembly of Proteins on Fluoride Ceramic (CeFACS applied bio materials · 2022Article
- Nanomedicines in the Management of Alzheimer's Disease: Current View and Future Prospects.Frontiers in aging neuroscience · 2022Review
- Nanomaterials for Modulating the Aggregation of β-Amyloid Peptides.Molecules (Basel, Switzerland) · 2021Review
- β-Amyloid Targeting with Two-Dimensional Covalent Organic Frameworks: Multi-Scale In-Silico Dissection of Nano-Biointerface.Chembiochem : a European journal of chemical biology · 2021Article
- "What Doesn't Kill You Makes You Stronger": Future Applications of Amyloid Aggregates in Biomedicine.Molecules (Basel, Switzerland) · 2020Review
- Structural Insight into the Interactions between Structurally Similar Inhibitors and SIRT6.International journal of molecular sciences · 2020Article
- Computational screening of nanoparticles coupling to Aβ40 peptides and fibrils.Scientific reports · 2019Article
- Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms.International journal of molecular sciences · 2018Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The abnormal self-assembly of the amyloid-β peptide into toxic β-rich aggregates can cause Alzheimer’s disease. Recently, it has been shown that small gold nanoparticles (AuNPs) inhibit Aβ aggregation and fibrillation by slowing down the nucleation process in experimental studies. However, the effects of AuNPs on Aβ oligomeric structures are still unclear. In this study, we investigate the conformation of Aβ(16-22) tetramers/octamers in the absence and presence of AuNPs using extensive all-atom molecular-dynamics simulations in explicit solvent. Our studies demonstrate that the addition of AuNPs into Aβ(16-22) solution prevents β-sheet formation, and the inhibition depends on the concentration of Aβ(16-22) peptides. A detailed analysis of the Aβ(16-22)/Aβ(16-22)/water/AuNPs interactions reveals that AuNPs inhibit the β-sheet formation resulting from the same physical forces: hydrophobic interactions. Overall, our computational study provides evidence that AuNPs are likely to inhibit Aβ(16-22) and full-length Aβ fibrillation. Thus, this work provides theoretical insights into the development of inorganic nanoparticles as drug candidates for treatment of AD.
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