Modulation of β-amyloid aggregation by graphene quantum dots
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...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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The Royal Society
2019-06-01
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| Series: | Royal Society Open Science |
| Subjects: | |
| Online Access: | https://royalsocietypublishing.org/doi/pdf/10.1098/rsos.190271 |
| _version_ | 1818205013980217344 |
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| author | Changliang Liu Huan Huang Lilusi Ma Xiaocui Fang Chen Wang Yanlian Yang |
| author_facet | Changliang Liu Huan Huang Lilusi Ma Xiaocui Fang Chen Wang Yanlian Yang |
| author_sort | Changliang Liu |
| collection | DOAJ |
| description | 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 (Aβ1–42) aggregation. GQDs displayed significant regulatory effects on the aggregation of Aβ1–42 peptide as detected by thioflavin T (ThT) assay. Then, the changes of confirmations and structures induced by GQDs on the Aβ1–42 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 Aβ1–42 aggregation. Meanwhile, the structural changes of a Aβ1–42/GQDs mixture in different pH revealed that electrostatic interaction was the major driving force in the co-assembly process of Aβ1–42 and GQDs. The proposed mechanism of the regulatory effects of GQDs on the Aβ1–42 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 Aβ1–42 aggregation. |
| first_indexed | 2024-12-12T03:50:23Z |
| format | Article |
| id | doaj.art-5fd7ce511e144026a4f44d82baee4880 |
| institution | Directory Open Access Journal |
| issn | 2054-5703 |
| language | English |
| last_indexed | 2024-12-12T03:50:23Z |
| publishDate | 2019-06-01 |
| publisher | The Royal Society |
| record_format | Article |
| series | Royal Society Open Science |
| spelling | doaj.art-5fd7ce511e144026a4f44d82baee48802022-12-22T00:39:24ZengThe Royal SocietyRoyal Society Open Science2054-57032019-06-016610.1098/rsos.190271190271Modulation of β-amyloid aggregation by graphene quantum dotsChangliang LiuHuan HuangLilusi MaXiaocui FangChen WangYanlian YangMisfolding 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 (Aβ1–42) aggregation. GQDs displayed significant regulatory effects on the aggregation of Aβ1–42 peptide as detected by thioflavin T (ThT) assay. Then, the changes of confirmations and structures induced by GQDs on the Aβ1–42 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 Aβ1–42 aggregation. Meanwhile, the structural changes of a Aβ1–42/GQDs mixture in different pH revealed that electrostatic interaction was the major driving force in the co-assembly process of Aβ1–42 and GQDs. The proposed mechanism of the regulatory effects of GQDs on the Aβ1–42 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 Aβ1–42 aggregation.https://royalsocietypublishing.org/doi/pdf/10.1098/rsos.190271graphene quantum dotsβ-amyloid aggregationmodulation |
| spellingShingle | Changliang Liu Huan Huang Lilusi Ma Xiaocui Fang Chen Wang Yanlian Yang Modulation of β-amyloid aggregation by graphene quantum dots Royal Society Open Science graphene quantum dots β-amyloid aggregation modulation |
| title | Modulation of β-amyloid aggregation by graphene quantum dots |
| title_full | Modulation of β-amyloid aggregation by graphene quantum dots |
| title_fullStr | Modulation of β-amyloid aggregation by graphene quantum dots |
| title_full_unstemmed | Modulation of β-amyloid aggregation by graphene quantum dots |
| title_short | Modulation of β-amyloid aggregation by graphene quantum dots |
| title_sort | modulation of β amyloid aggregation by graphene quantum dots |
| topic | graphene quantum dots β-amyloid aggregation modulation |
| url | https://royalsocietypublishing.org/doi/pdf/10.1098/rsos.190271 |
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