4.8 Article

High-Efficiency CdSe Quantum Dots/Fe3O4@MoS2/S2O82- Electrochemiluminescence System Based on a Microfluidic Analysis Platform for the Sensitive Detection of Neuron-Specific Enolase

Journal

ANALYTICAL CHEMISTRY
Volume -, Issue -, Pages -

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.2c01868

Keywords

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Funding

  1. National Natural Science Foundation of China [21777056, 21427808]
  2. Special Foundation for Taishan Scholar Professorship of Shandong Province
  3. Jinan Scientific Research Leader Workshop Project [2018GXRC024, 2018GXRC021]

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In this study, a sensing platform was developed for the quantitative detection of neuron-specific enolase using electrochemiluminescence technology and self-assembled portable disease detection chips. The platform demonstrated great potential in early tumor screening and clinical diagnosis, and the introduction of a short peptide ligand further improved the binding efficiency of antibodies and the activity of biosensors.
In this work, based on electrochemiluminescence (ECL) technology and self-assembled portable disease detection chips, a bioactivity-maintained sensing platform was developed for the quantitative detection of neuron-specific enolase. First, we prepared Fe3O4@MoS2 nanocomposites as an efficient catalyst to accelerate the reduction of persulfate (S2O82-). Specifically, abundant sulfate radicals (SO4 center dot-) were generated because of cyclic conversion between Fe2+ and Fe3+. Meanwhile, MoS2 nanoflowers with a high specific surface area could not only load more Fe3O4 but also solve its agglomeration problem, which greatly improved the catalytic efficiency. Moreover, a biosensor chip was constructed by standard lithography processes for disease detection, which had good sensitivity and portability. According to the above strategies, the developed portable sensing platform played the part of promoting the practical application of bioanalysis in early tumor screening and clinical diagnosis. In addition, we developed a short peptide ligand (NARKFYKG, NAR) to avoid the occupation of antigen binding sites by specifically connecting to Fc fragments in antibodies. Thus, the binding efficiency of antibodies and the activity of biosensors were improved due to the introduction of NAR.

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