4.3 Article

Preparation of IDA-Cu functionalized core-satellite Fe3O4/polydopamine/Au magnetic nanocomposites and their application for depletion of abundant protein in bovine blood

期刊

JOURNAL OF MATERIALS CHEMISTRY
卷 20, 期 47, 页码 10696-10704

出版社

ROYAL SOC CHEMISTRY
DOI: 10.1039/c0jm01336f

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资金

  1. 863 High Technology Project of China [2007AA10Z432]
  2. National Basic Research Program of China [2007CB914100]
  3. National Natural Science Foundation of China [20935001, 20675040, 20875050]
  4. Natural Science Foundation of Tianjin [10JCZDJC17600]

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In this study, we report a method to synthesize core-satellite structured Fe3O4/polydopamine/Au composite nanoparticles (NPs). Firstly, the Fe3O4/polydopamine composite NPs with a well-defined core-shell structure are obtained using dopamine self-polymerization to form thin, surface-adherent polydopamine films onto the surface of a Fe3O4 core. The polydopamine shell could be adjusted by controlling the experimental parameters such as reaction time and the reactant concentrations. Then, numerous satellites of gold nanoparticles were assembled on the surface of Fe3O4/polydopamine by reducing Au3+ between the Fe3O4/polydopamine solid and HAuCl4 solution. Next, 11-mercaptoundecanoic acid (11-MUA) forms a self-assembled monolayer of MUA on the surface of the Au NPs and polydopamine layer. Finally, IDA-Cu functionalized Fe3O4/polydopamine/Au composite NPs are obtained by the carboxyl groups of MUA reacting with iminodiacetic acid (IDA), charged with Cu2+. The IDA-Cu groups, acting as an anchor, are attached on the gold and the polydopamine surface is designed for capturing target molecules. The morphology, structure and composition of the nanocomposites are characterized by transmission electron microscopy (TEM), X-ray powder diffraction (XRD), Fourier transform infrared (FTIR) spectroscopy and X-ray photoelectron spectrometry (XPS). The resulting Fe3O4/polydopamine/Au composite NPs show not only a strong magnetic response to an externally applied magnetic field, but are also highly specific to protein bovine hemoglobin (BHb), and removal of abundant protein BHb in the bovine blood as well. This opens a novel route for future application in removing abundant protein in proteomic analysis.

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