Modulation of β-amyloid aggregation by graphene quantum dots
| Autor: | Lilusi Ma, Changliang Liu, Huan Huang, Chen Wang, Xiaocui Fang, Yanlian Yang |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Circular dichroism
Peptide 02 engineering and technology 010402 general chemistry 01 natural sciences law.invention chemistry.chemical_compound Dynamic light scattering β-amyloid aggregation law lcsh:Science chemistry.chemical_classification Multidisciplinary graphene quantum dots Graphene 021001 nanoscience & nanotechnology 0104 chemical sciences Chemistry modulation chemistry Modulation Transmission electron microscopy Quantum dot Biophysics Thioflavin lcsh:Q 0210 nano-technology Research Article |
| Zdroj: | Royal Society Open Science, Vol 6, Iss 6 (2019) Royal Society Open Science |
| ISSN: | 2054-5703 |
| DOI: | 10.1098/rsos.190271 |
| Popis: | Misfolding and abnormal aggregation of β-amyloid peptide is associated with the onset and progress of Alzheimer's disease (AD). Therefore, modulating β-amyloid aggregation is critical for the treatment of AD. Herein, we studied the regulatory effects and mechanism of graphene quantum dots (GQDs) on 1–42 β-amyloid (Aβ 1–42 ) aggregation. GQDs displayed significant regulatory effects on the aggregation of Aβ 1–42 peptide as detected by thioflavin T (ThT) assay. Then, the changes of confirmations and structures induced by GQDs on the Aβ 1–42 aggregation were monitored by circular dichroism (CD), dynamic light scattering (DLS) and transmission electron microscope (TEM). The in vitro cytotoxicity experiments further demonstrated the feasibility of GQDs on the regulation of Aβ 1–42 aggregation. Meanwhile, the structural changes of a Aβ 1–42 /GQDs mixture in different pH revealed that electrostatic interaction was the major driving force in the co-assembly process of Aβ 1–42 and GQDs. The proposed mechanism of the regulatory effects of GQDs on the Aβ 1–42 aggregation was also deduced reasonably. This work not only demonstrated the potential feasibility of GQDs as therapeutic drug for AD but also clarified the regulatory mechanism of GQDs on the Aβ 1–42 aggregation. |
| Databáze: | OpenAIRE |
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