ArticleNanoscale advances2020
Tyrosine carbon dots inhibit fibrillation and toxicity of the human islet amyloid polypeptide.
Article in Nanoscale advances, 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, 19 citations in OpenAlex.
- Review
- Copper and Nitrogen Co-doped Fluorescent Carbon Quantum Dots as a Fluorescent ''turn-off" Sensor for Determination of Tetracyclines Antibiotics.Journal of fluorescence · 2026Article
- L-tyrosine inhibits the formation of amyloid fibers of human lysozyme at physiological pH and temperature.Amino acids · 2025Article
- Flavones in pomelo peel resist fibril formation of human islet amyloid polypeptide.Chinese herbal medicines · 2025Article
- Carboxylic Group Functionalized Carbon Quantum Dots inhibit Hen Egg White Lysozyme Amyloidogenesis, leading to the Formation of Spherical Aggregates with Reduced Toxicity and ROS Generation.Current protein & peptide science · 2024Article
- Scavenging neurotoxic aldehydes using lysine carbon dots.Nanoscale advances · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Misfolding and aggregation of the human islet amyloid polypeptide (hIAPP) are believed to play key roles in the pathophysiology of type-II diabetes. Here, we demonstrate that carbon dots (C-dots) prepared from the amino acid tyrosine inhibit fibrillation of hIAPP, reduce hIAPP-induced cell toxicity and block membrane disruption by the peptide. The pronounced inhibitory effect is traced to the display of ubiquitous aromatic residues upon the C-dots' surface, mimicking the anti-fibril and anti-toxic activity of natural polyphenolic compounds. Notably, spectroscopy and thermodynamics analysis demonstrated different hIAPP interactions and fibril inhibition effects induced by tyrosine-C-dots displaying phenolic residues and C-dots prepared from phenylalanine which exhibited phenyl units on their surface, underscoring the significance of hydrogen bonding mediated by the phenolic hydroxide moieties for the fibril modulation activity. The presented experiments attest to the potential of tyrosine-C-dots as a therapeutic vehicle for protein misfolding diseases, interfering in both π-π interactions as well as hydrogen bonding involving aromatic residues of amyloidogenic peptides.
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Registered trials
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