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20241210232718.0 |
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241128s2024 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.4c03454
|2 doi
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|a pubmed24n1627.xml
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|a (DE-627)NLM380888025
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|a (NLM)39602498
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|a DE-627
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|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Chen, Shenna
|e verfasserin
|4 aut
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| 245 |
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|a Multifunctional Nitrogen-Doped Carbon Dots to Inhibit the Aggregation of Aβ Peptide and Depolymerize the Aβ Fibrils by Modulating Reactive Oxygen Species
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|c 2024
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 10.12.2024
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|a Date Revised 10.12.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Multifunctional nitrogen-doped carbon dots (N-CDs) were synthesized, and the morphology, composition, and spectral properties of N-CDs were characterized by multiple characterization techniques. The inhibition of β-amyloid (Aβ) peptide aggregation and the destruction of the Aβ fibril structure by N-CDs were also studied. The conformational transition and morphology of Aβ42 in the presence of N-CDs were monitored by far-UV circular dichroism (CD) spectroscopy and transmission electron microscopy (TEM). The results demonstrated that the prepared N-CDs could effectively inhibit Aβ42 peptide aggregation and depolymerize Aβ fibrils. Furthermore, the inhibition and disaggregation mechanism of existing Aβ42 fibrils by N-CDs was studied by electron paramagnetic resonance spectroscopy (EPR). The results showed that the modulation of reactive oxygen species (ROS) by N-CDs and multiple interactions between N-CDs and Aβ42 fibrils played a crucial part in restraining and reducing the aggregation of Aβ42. Our work demonstrates the therapeutic potential of N-CDs in suppressing Aβ42 peptide aggregation and destroying existing Aβ42 fibrils, which provides a new perspective strategy in the treatment of Alzheimer's disease (AD)
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|a Journal Article
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|a Amyloid beta-Peptides
|2 NLM
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|a Nitrogen
|2 NLM
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|a N762921K75
|2 NLM
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| 650 |
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|a Reactive Oxygen Species
|2 NLM
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| 650 |
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|a Carbon
|2 NLM
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| 650 |
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|a 7440-44-0
|2 NLM
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| 650 |
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|a Protein Aggregates
|2 NLM
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|a amyloid beta-protein (1-42)
|2 NLM
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| 650 |
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|a Peptide Fragments
|2 NLM
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| 700 |
1 |
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|a Li, Ronghui
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Liu, Yanxu
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhang, Ziyan
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Fang, Mei
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Huang, Sihang
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Li, Yayong
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Geng, Lina
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1999
|g 40(2024), 49 vom: 10. Dez., Seite 26018-26025
|w (DE-627)NLM098181009
|x 1520-5827
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| 773 |
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|g volume:40
|g year:2024
|g number:49
|g day:10
|g month:12
|g pages:26018-26025
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|u http://dx.doi.org/10.1021/acs.langmuir.4c03454
|3 Volltext
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