Intermolecular B-N coordination and multi-interaction synergism induced selective glycoprotein adsorption by phenylboronic acid-functionalized magnetic composites under acidic and neutral conditions.
Intermolecular B-N coordination and multi-interaction synergism induced selective glycoprotein adsorption by phenylboronic acid-functionalized magnetic composites under acidic and neutral conditions.
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DOI：
10.1039/d0tb01901a
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发表时间：
2020-10
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影响因子：
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通讯作者：
Zhiyu Li;Bin Luo;Lingzhu Yu;Fang Lan;Yao Wu
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文献类型：
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作者：
Zhiyu Li;Bin Luo;Lingzhu Yu;Fang Lan;Yao Wu
异常蛋白质糖基化与许多疾病相关，包括心血管疾病、糖尿病和癌症。因此，在生理或弱酸条件下（肿瘤微环境）选择性捕获糖蛋白对于疾病诊断和进一步的综合分析至关重要。在这里，我们提出了一种策略，分子间的B-N键为基础的苯硼酸亲和捕获糖蛋白在中性和微酸性条件下。令人惊讶的是，捕获的糖蛋白在碱性溶液中释放。这与传统的苯硼酸亲和性相反，我们从材料、蛋白质和孵育条件的角度对此进行了研究。我们确定了在微酸性条件下，分子间B-N键的苯硼酸亲和性，静电相互作用和聚合物刷结构的糖蛋白吸附的协同效应。Fe3O4@SiO2@聚甲基丙烯酸2-氨乙酯盐酸盐（PAMA-CPBA）纳米粒子与转铁蛋白（TRF）之间的静电排斥作用远大于CPBA的苯硼酸与TRF糖基化残基之间的特异性结合作用，导致捕获的糖蛋白在碱性溶液中释放。Fe3O4@SiO2@PAMA-CPBA纳米粒子在多蛋白溶液中由于蛋白质相互作用而对不同的糖蛋白表现出不同的选择性。这些结果可能为设计苯硼酸基材料在生理环境中对糖蛋白的吸附铺平了新的道路。
Abnormal protein glycosylation is associated with many diseases including cardiovascular disease, diabetes, and cancer. Therefore, selective capturing of glycoproteins under physiological or weak acid conditions (tumor microenvironment) is vital for disease diagnosis and further comprehensive analysis. Here, we propose a strategy of intermolecular B-N bond-based phenylboronic acid affinity to capture glycoproteins under neutral and slightly acidic conditions. Surprisingly, the captured glycoproteins were released in alkaline solution. This is contrary to the traditional phenylboric acid affinity, and we studied this from the perspective of materials, proteins, and incubation conditions. We identified the synergistic effect of intermolecular B-N bond-based phenylboronic acid affinity, electrostatic interaction, and polymer brush structure-based glycoprotein adsorption under slightly acidic conditions. The electrostatic repulsion between Fe3O4@SiO2@poly (2-aminoethyl methacrylate hydrochloride)-4-carboxyphenylboronic acid (Fe3O4@SiO2@PAMA-CPBA) nanoparticles and transferrin (TRF) was far greater than the specific binding between phenylboric acid of CPBA and glycosylation residues of TRF resulting in the release of the captured glycoproteins in alkaline solution. Fe3O4@SiO2@PAMA-CPBA nanoparticles exhibited different selectivity capabilities toward different glycoproteins in multiprotein solutions due to protein interactions. These results may pave a new way for the design of phenylboric acid-based materials towards glycoprotein adsorption in a physiological environment.