ArticleThe journal of physical chemistry. C, Nanomaterials and interfaces2017
Gold Nanoparticles as a Probe for Amyloid-β Oligomer and Amyloid Formation.
Article in The journal of physical chemistry. C, Nanomaterials and interfaces, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The trial behind it
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Who cites it
20 citing papers in PubMed.
- Nano-based spectroscopic approaches for early diagnosis of Alzheimer's disease: critical insights into amyloid-β and tau biomarker biology and detection tools.Biophysical reviews · 2026Review
- Neurogenesis and neuroplasticity activities of natural products: therapeutic potential in Alzheimer's disease.Frontiers in pharmacology · 2026Review
- Nanomaterials in targeting amyloid-β oligomers: current advances and future directions for Alzheimer's disease diagnosis and therapy.Beilstein journal of nanotechnology · 2025Review
- Gold Nanoparticles in Neurological Diseases: A Review of Neuroprotection.International journal of molecular sciences · 2024Review
- Functional Nanomaterials for the Diagnosis of Alzheimer's Disease: Recent Progress and Future Perspectives.Advanced functional materials · 2023Article
- Gold and silver nanoparticles in Alzheimer's and Parkinson's diagnostics and treatments.Ibrain · 2023Review
- Astrocytic MicroRNAs and Transcription Factors in Alzheimer's Disease and Therapeutic Interventions.Cells · 2022Review
- Mucin-TypeFrontiers in chemistry · 2022Article
- Clinical relevance of biomarkers, new therapeutic approaches, and role of post-translational modifications in the pathogenesis of Alzheimer's disease.Frontiers in aging neuroscience · 2022Review
- Nanomedicines in the Management of Alzheimer's Disease: Current View and Future Prospects.Frontiers in aging neuroscience · 2022Review
- Research Models of the Nanoparticle-Mediated Drug Delivery across the Blood-Brain Barrier.Tissue engineering and regenerative medicine · 2021Review
- Effects of the Hydrophilic N-Terminal Region on Aβ-Mediated Membrane Disruption.The journal of physical chemistry. B · 2021Article
- Potential Role of Nanoparticles in Treating the Accumulation of Amyloid-Beta Peptide in Alzheimer's Patients.Polymers · 2021Review
- Plasmonic Nanoparticles as Optical Sensing Probes for the Detection of Alzheimer's Disease.Sensors (Basel, Switzerland) · 2021Review
- Au nano-urchins enabled localized surface plasmon resonance sensing of beta amyloid fibrillation.Nanoscale advances · 2020Article
- Improving Sensitivity and Specificity of Amyloid-β Peptides and Tau Protein Detection with Antibiofouling Magnetic Nanoparticles for Liquid Biopsy of Alzheimer's Disease.ACS biomaterials science & engineering · 2019Article
- Aβ42 fibril formation from predominantly oligomeric samples suggests a link between oligomer heterogeneity and fibril polymorphism.Royal Society open science · 2019Article
- Electrochemiluminescence of gold nanoparticles and gold nanoparticle-labelled antibodies as co-reactants.RSC advances · 2018Article
- Magnetic Nanoparticles Applications for Amyloidosis Study and Detection: A Review.Nanomaterials (Basel, Switzerland) · 2018Review
- N-Terminal Charged Residues of Amyloid-β Peptide Modulate Amyloidogenesis and Interaction with Lipid Membrane.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The process of amyloid-β (Aβ) amyloid formation is pathologically linked to Alzheimer's disease (AD). The identification of Aβ amyloids and intermediates that are crucial players in the pathology of AD is critical for exploring the underlying mechanism of Aβ aggregation and the diagnosis of the disease. Herein, we performed a gold nanoparticle (AuNP)-based study to detect the formation of Aβ amyloid fibrils and oligomers. Our results demonstrate that the intensity of the surface plasmon resonance (SPR) absorption band of the AuNPs is sensitive to the quantity of Aβ40 amyloids. This allows the SPR assay to be used for detection and semi-quantification of Aβ40 amyloids, and characterization of the kinetics of Aβ amyloid formation. Furthermore, our study demonstrates that the SPR band intensity of the AuNPs is sensitive to the presence of oligomers of both Aβ40 and an Aβ40 mutant, which forms more stable oligomers. The kinetics of the stable oligomer formation of the Aβ40 mutant can also be monitored following the SPR band intensity change of AuNPs. Our results indicate that this nanoparticle based method can be used for mechanistic studies of early protein self-assembly and fibrillogenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.