Cited by 58Alzheimer's disease research and treatmentsCarbon and Quantum Dots ApplicationsCholinesterase and Neurodegenerative Diseases

Synergistic Inhibitory Effect of GQDs–Tramiprosate Covalent Binding on Amyloid Aggregation

Liu, Yibiao, Xu, Li-Ping, Wang, Qiang, Yang, Baocheng, Zhang, Xueji·2018·ACS Chemical Neuroscience

Abstract

Inhibiting the amyloid aggregation is considered to be an effective strategy to explore possible treatment of amyloid-related diseases including Alzheimer's disease, Parkinson's disease, and type II diabetes. Herein, a new high-efficiency and low-cytotoxicity Aβ aggregation inhibitors, GQD-T, was designed through the combination of two Aβ aggregation inhibitors, graphene quantum dots (GQDs) and tramiprosate. GQD-T showed the capability of efficiently inhibiting the aggregation of Aβ peptides and rescuing Aβ-induced cytotoxicity due to the synergistic effect of the GQDs and tramiprosate. In addition, the GQD-T has the characteristics of low toxicity and great biocompatibility. It is believed that GQD-T may be a potential candidate for an Alzheimer's drug and this work provides a new strategy for exploring Aβ peptide aggregation inhibitors.

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Crossref · 10.1021/acschemneuro.7b00439

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2 of 2 references verified0 citation errors · 0 not checkable

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  • QDs possess stable fluorescence, allowing imaging of amyloid aggregates; tramiprosate inhibits Aβ aggregation, acting on different parts of the pathological cascade.

    “The QD themselves possess stable fluorescence, which allows them to be used for imaging amyloid aggregates. Tramiprosate, in turn, inhibits Aβ aggregation, acting on different parts of the pathological cascade.”
  • The pharmacokinetics of the graphene QD-tramiprosate system is determined by the nanocarrier, which ensures delivery of both components across the BBB and their joint accumulation in the target area.

    “The pharmacokinetics of such a system is determined by the nanocarrier, which ensures the delivery of both components across the BBB and their joint accumulation in the target area [87].”
  • The first approach-combining functions in a single agent-is implemented in systems based on graphene QDs conjugated with tramiprosate.

    “The first approach—combining functions in a single agent—is implemented, in particular, in systems based on graphene QDs conjugated with tramiprosate.”

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Authors
Liu, Y., Xu, L.-P., Wang, Q., Yang, B., & Zhang, X.
Affiliations
  • Huanghe Science and Technology College (CN)
  • Research Center for Bioengineering and Sensing Technology, University of Science & Technology Beijing, Beijing 100083, P.R. China
  • Chinese Academy of Sciences (CN)
  • University of Science and Technology Beijing (CN)
Corresponding author
Yang, Baocheng
Venue
ACS Chemical Neuroscience
Published
2017-12-15
Volume
9
Issue
4
Pages
817-823
ISSN
1948-7193 (ISSN-L)
OpenAlex
W2775268498
Cited by
58
References
2
Citations by year
2026: 4 · 2025: 9 · 2024: 5 · 2023: 6 · 2022: 8 · 2021: 9 · 2020: 9 · 2019: 3 · 2018: 5
FWCI
3.44
Type
journal article
Language
en
Open access
closed
Locations
  • ACS Chemical Neuroscience (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Natural Science Foundation of China (21475009, 21475008)
  • Beijing Municipal Science and Technology Commission (Z161100000116037)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Physical Sciences › Materials Science › Materials Chemistry › Carbon and Quantum Dots Applications
  • Health Sciences › Medicine › Pharmacology › Cholinesterase and Neurodegenerative Diseases
Keywords
graphene quantum dots, tramiprosate, amyloid aggregation inhibition, amyloid-beta, Alzheimer's disease, synergistic inhibition, covalent binding, cytotoxicity, biocompatibility, amyloidosis
MeSH terms
Alzheimer Disease, Amyloidosis, Diabetes Mellitus, Type 2, Graphite, Humans, Peptide Fragments, Taurine, Amyloid beta-Peptides, Quantum Dots, Amyloidogenic Proteins

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