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Rational Design of Nitrogen-Doped Carbon Dots for Inhibiting β-Amyloid Aggregation
The fibrillization and abnormal aggregation of β-amyloid (Aβ) peptides are commonly recognized risk factors for Alzheimer’s disease (AD) brain, and require an effective strategy to inhibit the Aβ deposition and treat AD. Herein, we designed and synthesized nitrogen-doped carbon dots (N-CDs) as an Aβ...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9919344/ https://www.ncbi.nlm.nih.gov/pubmed/36771112 http://dx.doi.org/10.3390/molecules28031451 |
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author | Liu, Hong Guo, Huazhang Fang, Yibin Wang, Liang Li, Peng |
author_facet | Liu, Hong Guo, Huazhang Fang, Yibin Wang, Liang Li, Peng |
author_sort | Liu, Hong |
collection | PubMed |
description | The fibrillization and abnormal aggregation of β-amyloid (Aβ) peptides are commonly recognized risk factors for Alzheimer’s disease (AD) brain, and require an effective strategy to inhibit the Aβ deposition and treat AD. Herein, we designed and synthesized nitrogen-doped carbon dots (N-CDs) as an Aβ-targeted probe, which exhibits the capacity of inhibiting the 1–42 Aβ (Aβ(1–42)) self-assembly in vitro. The N-CDs exhibited orange emission with an emission wavelength of 570 nm, which demonstrates their excellent optical properties with excitation-independent behavior. Meanwhile, the N-CDs have spherical morphologies with an average size of 2.2 nm, whose surface enriches the amino, carboxyl, and hydroxyl groups. These preparties are conducive to improving their biological water solubility and provide a large number of chemical bonds for further interaction with proteins. Contrary to this, the kinetic process, size evolutions, and morphologies changes of Aβ(1–42) were inhibited in the presence of N-CDs in the determination of a thioflavin T assay, dynamic light scattering, transmission electron microscope, etc. Finally, the safety application of N-CDs on Aβ(1–42)-induced cytotoxicity was further demonstrated via in vitro cytotoxicity experiments. This work demonstrates the effective outcome of suppressing Aβ aggregation, which provides a new view into the high-efficiency and low-cytotoxicity strategy in AD theranostics. |
format | Online Article Text |
id | pubmed-9919344 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-99193442023-02-12 Rational Design of Nitrogen-Doped Carbon Dots for Inhibiting β-Amyloid Aggregation Liu, Hong Guo, Huazhang Fang, Yibin Wang, Liang Li, Peng Molecules Communication The fibrillization and abnormal aggregation of β-amyloid (Aβ) peptides are commonly recognized risk factors for Alzheimer’s disease (AD) brain, and require an effective strategy to inhibit the Aβ deposition and treat AD. Herein, we designed and synthesized nitrogen-doped carbon dots (N-CDs) as an Aβ-targeted probe, which exhibits the capacity of inhibiting the 1–42 Aβ (Aβ(1–42)) self-assembly in vitro. The N-CDs exhibited orange emission with an emission wavelength of 570 nm, which demonstrates their excellent optical properties with excitation-independent behavior. Meanwhile, the N-CDs have spherical morphologies with an average size of 2.2 nm, whose surface enriches the amino, carboxyl, and hydroxyl groups. These preparties are conducive to improving their biological water solubility and provide a large number of chemical bonds for further interaction with proteins. Contrary to this, the kinetic process, size evolutions, and morphologies changes of Aβ(1–42) were inhibited in the presence of N-CDs in the determination of a thioflavin T assay, dynamic light scattering, transmission electron microscope, etc. Finally, the safety application of N-CDs on Aβ(1–42)-induced cytotoxicity was further demonstrated via in vitro cytotoxicity experiments. This work demonstrates the effective outcome of suppressing Aβ aggregation, which provides a new view into the high-efficiency and low-cytotoxicity strategy in AD theranostics. MDPI 2023-02-02 /pmc/articles/PMC9919344/ /pubmed/36771112 http://dx.doi.org/10.3390/molecules28031451 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Communication Liu, Hong Guo, Huazhang Fang, Yibin Wang, Liang Li, Peng Rational Design of Nitrogen-Doped Carbon Dots for Inhibiting β-Amyloid Aggregation |
title | Rational Design of Nitrogen-Doped Carbon Dots for Inhibiting β-Amyloid Aggregation |
title_full | Rational Design of Nitrogen-Doped Carbon Dots for Inhibiting β-Amyloid Aggregation |
title_fullStr | Rational Design of Nitrogen-Doped Carbon Dots for Inhibiting β-Amyloid Aggregation |
title_full_unstemmed | Rational Design of Nitrogen-Doped Carbon Dots for Inhibiting β-Amyloid Aggregation |
title_short | Rational Design of Nitrogen-Doped Carbon Dots for Inhibiting β-Amyloid Aggregation |
title_sort | rational design of nitrogen-doped carbon dots for inhibiting β-amyloid aggregation |
topic | Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9919344/ https://www.ncbi.nlm.nih.gov/pubmed/36771112 http://dx.doi.org/10.3390/molecules28031451 |
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