ArticlePhysical chemistry chemical physics : PCCP2016
Graphene oxide inhibits hIAPP amyloid fibrillation and toxicity in insulin-producing NIT-1 cells.
Article in Physical chemistry chemical physics : PCCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 79 citations in OpenAlex.
- Exploring 2D Graphene-Based Nanomaterials for Biomedical Applications: A Theoretical Modeling Perspective.Small science · 2025Article
- Evaluation of pancreatic δ- cells as a potential target site of graphene oxide toxicity in Japanese medaka (Oryzias latipes) fish.Ecotoxicology and environmental safety · 2023Article
- Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models.International journal of molecular sciences · 2022Review
- Ginkgo biloba in the management of the COVID-19 severity.Archiv der Pharmazie · 2022Review
- Melatonin Inhibits hIAPP Oligomerization by Preventing β-Sheet and Hydrogen Bond Formation of the Amyloidogenic Region Revealed by Replica-Exchange Molecular Dynamics Simulation.International journal of molecular sciences · 2022Article
- Human islet amyloid polypeptide: A therapeutic target for the management of type 2 diabetes mellitus.Journal of pharmaceutical analysis · 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
- Recent advances of two-dimensional materials in smart drug delivery nano-systems.Bioactive materials · 2020Review
- Amyloidosis Inhibition, a New Frontier of the Protein Corona.Nano today · 2020Article
- Interfacial charge transfer with exfoliated graphene inhibits fibril formation in lysozyme amyloid.Biointerphases · 2020Article
- Pristine and Hydroxylated Fullerenes Prevent the Aggregation of Human Islet Amyloid Polypeptide and Display Different Inhibitory Mechanisms.Frontiers in chemistry · 2020Article
- Role of surface oxygen-containing functional groups of graphene oxide quantum dots on amyloid fibrillation of two model proteins.PloS one · 2020Article
- Amphiphilic surface chemistry of fullerenols is necessary for inhibiting the amyloid aggregation of alpha-synuclein NACore.Nanoscale · 2019Article
- Nucleation of β-rich oligomers and β-barrels in the early aggregation of human islet amyloid polypeptide.Biochimica et biophysica acta. Molecular basis of disease · 2019Article
- Evaluation of the photo-degradation of Alzheimer's amyloid fibrils with a label-free approach.Chemical communications (Cambridge, England) · 2018Article
- Article
- Nanoscale inhibition of polymorphic and ambidextrous IAPP amyloid aggregation with small molecules.Nano research · 2018Article
- Dual effect of PEG-PE micelle over the oligomerization and fibrillation of human islet amyloid polypeptide.Scientific reports · 2018Article
- Star Polymers Reduce Islet Amyloid Polypeptide Toxicity via Accelerated Amyloid Aggregation.Biomacromolecules · 2017Article
- Implications of peptide assemblies in amyloid diseases.Chemical Society reviews · 2017Review
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Authors and funding
9 authors at 6 institutions in 3 countries.
Funding
Abstract
Human islet amyloid polypeptide (hIAPP or amylin) aggregation is directly associated with pancreatic β-cell death and subsequent insulin deficiency in type 2 diabetes (T2D). Since no cure is currently available for T2D, it is of great benefit to devise new anti-aggregation molecules, which protect β-cells against hIAPP aggregation-induced toxicity. Engineered nanoparticles have been recently exploited as anti-aggregation nanomedicines. In this work, we studied graphene oxide (GO) nanosheets for their potential for hIAPP aggregation inhibition by combining computational modeling, biophysical characterization and cell toxicity measurements. Using discrete molecular dynamics (DMD) simulations and in vitro studies, we showed that GO exhibited an inhibitory effect on hIAPP aggregation. DMD simulations indicated that the strong binding of hIAPP to GO nanosheets was driven by hydrogen bonding and aromatic stacking and that the strong peptide-GO binding efficiently inhibited hIAPP self-association and aggregation on the nanosheet surface. Secondary structural changes of hIAPP upon GO binding derived from DMD simulations were consistent with circular dichroism (CD) spectroscopy measurements. Transmission electron microscopy (TEM) images confirmed the reduction of hIAPP aggregation in the presence of GO. Furthermore, we carried out a cell toxicity assay and found that these nanosheets protected insulin-secreting NIT-1 pancreatic β-cells against hIAPP-induced toxicity. Our multidisciplinary study suggests that GO nanosheets have the potential to be utilized as an anti-aggregation nanomedicine itself in addition to a biosensor or delivery vehicle for the mitigation of T2D progression.
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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.