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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...

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Autores principales: Liu, Hong, Guo, Huazhang, Fang, Yibin, Wang, Liang, Li, Peng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
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.
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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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