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5 years ago

Carbon Nanodot-Sensitized Modulation of Alzheimer's β-Amyloid Self-Assembly, Disassembly, and Toxicity

Carbon Nanodot-Sensitized Modulation of Alzheimer's β-Amyloid Self-Assembly, Disassembly, and Toxicity
Kayoung Kim, Byung Il Lee, Chan Beum Park, You Jung Chung
The self-assembly of amyloidogenic peptides into β-sheet-rich aggregates is a general feature of many neurodegenerative diseases, including Alzheimer's disease, which signifies the need for the effective attenuation of amyloid aggregation toward alleviating amyloid-associated neurotoxicity. This study reports that photoluminescent carbon nanodots (CDs) can effectively suppress Alzheimer's β-amyloid (Aβ) self-assembly and function as a β-sheet breaker disintegrating preformed Aβ aggregates. This study synthesizes CDs using ammonium citrate through one-pot hydrothermal treatment and passivates their surface with branched polyethylenimine (bPEI). The bPEI-coated CDs (bPEI@CDs) exhibit hydrophilic and cationic surface characteristics, which interact with the negatively charged residues of Aβ peptides, suppressing the aggregation of Aβ peptides. Under light illumination, bPEI@CDs display a more pronounced effect on Aβ aggregation and on the dissociation of β-sheet-rich assemblies through the generation of reactive oxygen species from photoactivated bPEI@CDs. The light-triggered attenuation effect of Aβ aggregation using a series of experiments, including photochemical and microscopic analysis, is verified. Furthermore, the cell viability test confirms the ability of photoactivated bPEI@CDs for the suppression of Aβ-mediated cytotoxicity, indicating bPEI@CDs' potency as an effective anti-Aβ neurotoxin agent. Carbon nanodots (CDs) suppress Alzheimer's β-amyloid (Aβ) self-assembly and function as an antiamyloidogenic, β-sheet breaker to disintegrate preformed Aβ aggregates. The branched polyethylenimine (bPEI)-coated CDs (bPEI@CDs) induce higher hindrance on Aβ aggregation compared to bare CDs. Under light illumination, bPEI@CDs display more pronounced effects on Aβ aggregation inhibition and the dissociation of β-sheet-rich assemblies through generating reactive oxygen species.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/smll.201700983

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