ArticleiScience2020
Nontoxic Black Phosphorus Quantum Dots Inhibit Insulin Amyloid Fibrillation at an Ultralow Concentration.
Article in iScience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Polyol-Functionalized Manganese-Based Nanoparticles: From Insulin Amyloid Inhibition to Nanozyme-Mediated Antioxidant Activity.International journal of molecular sciences · 2026Article
- Advanced nanomaterials for modulating Alzheimer's related amyloid aggregation.Nanoscale advances · 2022Review
- Insulin-incubated palladium clusters promote recovery after brain injury.Journal of nanobiotechnology · 2022Article
- Recent Advances in the Treatment of Alzheimer's Disease Using Nanoparticle-Based Drug Delivery Systems.Pharmaceutics · 2022Review
- Oligomeric procyanidins inhibit insulin fibrillation by forming unstructured and off-pathway aggregates.RSC advances · 2021Article
- Recent advances in the biomedical applications of black phosphorus quantum dots.Nanoscale advances · 2021Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid are protein aggregates formed by cross β structures assemblies. Inhibiting amyloid aggregation or facilitating its disassembly are considered to be two major effective therapeutic strategies in diseases involving peptide or protein fibrillation such Alzheimer's disease or diabetes. Using thioflavin-T fluorescence, far-UV circular dichroism spectroscopy, and atomic force microscopy, we found nontoxic and biocompatible black phosphorus quantum dots (BPQDs) appear to have an exceptional capacity to inhibit insulin aggregation and to disassemble formed mature fibrils, even at an ultralow concentration (100 ng/mL). The inhibition of fibrillation persists at all stages of insulin aggregation and increases PC12 cells survival when exposed to amyloid fibrils. Molecular dynamics simulations suggest that BPQDs are able to stabilize the α-helix structure of insulin and obliterate the β-sheet structure to promote the fibril formation. These characteristics make BPQDs be promising candidate in preventing amyloidosis, disease treatment, as well as in the storage and processing of insulin.
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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 Socratic graph.