Jing Zhang, Xing Jia, Hong Qing and Hai-Yan Xie
Steady labeling of amyloid beta (Aβ) is crucial for studying the ingestion and degradation of Aβ by astrocytes and unraveling a relevant regulation mechanism. Quantum dots (QDs) are an optimum labeling reagent for this because of their strong and steady fluorescence properties. In this paper, Aβ was labeled with QDs by a simple mixed incubation strategy, with a QD labeled Aβ complex (QDs-Aβ) being obtained. In the complex, QDs efficiently restrained the formation of β-folding and fibrils of Aβ, while the graininess, dispersivity and fluorescence properties of the QDs hardly changed. The fluorescence microscopy imaging results showed that the astrocytes could ingest the QDs-Aβ. The QDs and Aβ did not separate from each other during the ingestion process, and the Aβ could be degraded subsequently.
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Steady labeling of amyloid beta (Aβ) is crucial for studying the ingestion and degradation of Aβ by astrocytes and unraveling a relevant regulation mechanism. Quantum dots (QDs) are an optimum labeling reagent for this because of their strong and steady fluorescence properties. In this paper, Aβ was labeled with QDs by a simple mixed incubation strategy, with a QD labeled Aβ complex (QDs-Aβ) being obtained. In the complex, QDs efficiently restrained the formation of β-folding and fibrils of Aβ, while the graininess, dispersivity and fluorescence properties of the QDs hardly changed. The fluorescence microscopy imaging results showed that the astrocytes could ingest the QDs-Aβ. The QDs and Aβ did not separate from each other during the ingestion process, and the Aβ could be degraded subsequently.
Link to full article
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