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

X射线光电子能谱 纳米复合材料 傅里叶变换红外光谱 材料科学 纳米颗粒 单层 化学工程 透射电子显微镜 复合数 表面改性 纳米技术 复合材料 工程类
作者
Min Zhang,Xiwen He,Langxing Chen,Yukui Zhang
出处
期刊:Journal of Materials Chemistry [The Royal Society of Chemistry]
卷期号:20 (47): 10696-10696 被引量:134
标识
DOI:10.1039/c0jm01336f
摘要

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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