Preparation of polymeric monoliths by copolymerization of acrylate monomers with amine functionalities for anion-exchange capillary liquid chromatography of proteins
Preparation of polymeric monoliths by copolymerization of acrylate monomers with amine functionalities for anion-exchange capillary liquid chromatography of proteins
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DOI：
10.1016/j.chroma.2009.05.037
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发表时间：
2009-07-17
影响因子：
4.1
通讯作者：
Lee, Milton L.
中科院分区：
文献类型：
--
作者：
Li, Yun;Gu, Binghe;Lee, Milton L.
通过甲基丙烯酸二乙氨基乙酯与聚乙二醇二丙烯酸酯(PEGDA)或丙烯酰氧基乙基三甲基氯化铵(PEGDA)与聚乙二醇二丙烯酸酯(PEGDA)的简单光引发共聚反应，在选定的致孔剂存在下，一步合成了两种新型的蛋白质阴离子交换毛细管液相色谱整体柱。得到的单体分别含有二乙氨基乙基(DEAE)作为弱阴离子交换剂和季胺作为强阴离子交换剂的官能团。通过光引发甲基丙烯酸缩水甘油酯(GMA)与聚乙二醇二乙二胺(PEGDA)的光引发共聚反应，合成了一种具有DEAE功能的弱阴离子交换整体柱。对合成的整体柱的重要物理性质和色谱学性质进行了表征。测定了三种固定相的动态结合容量(24 mg/mL.柱体积分别为56毫克/毫升和32毫克/毫升)与已报道的各种其他整体柱的值相当或更好。层析性能也类似于改性聚(GMA-乙二醇二甲基丙烯酸酯)整体柱。利用这些整体柱在梯度洗脱条件下实现了标准蛋白质的分离。分析时间为20~30min，得到了34、58和36个蛋白质的峰容量。这项工作代表了通过单体的直接共聚制备具有所需官能化的单体的成功尝试。与以前的文献相比，避免了额外的表面修饰，PEGDA交联剂有助于改善整体式主干的生物相容性。(C)2009爱思唯尔B.V.保留所有权利。
Two novel polymeric monoliths for anion-exchange capillary liquid chromatography of proteins were prepared in a single step by a simple photoinitiated copolymerization of 2-(diethylamino)ethyl methacrylate and polyethylene glycol diacrylate (PEGDA), or copolymerization of 2-(acryloyloxy)ethyl trimethylammonium chloride and PEGDA, in the presence of selected porogens. The resulting monoliths contained functionalities of diethylaminoethyl (DEAE) as a weak anion-exchanger and quaternary amine as a strong anion-exchanger, respectively. An alternative weak anion-exchange monolith with DEAE functionalities was also synthesized by chemical modification after photoinitiated copolymerization of glycidyl methacrylate (GMA) and PEGDA. Important physical and chromatographic properties of the synthesized monoliths were characterized. The dynamic binding capacities of the three monoliths (24 mg/mL. 56 mg/mL and 32 mg/mL Of column volume, respectively) were comparable or superior to Values that have been reported for Various other monoliths. Chromatographic performance was also similar to that provided by a modified poly(GMA-ethylene glycol dimethacrylate) monolith. Separation of standard proteins was achieved under gradient elution conditions using these monolithic columns. Peak capacities of 34, 58 and 36 proteins were obtained with analysis times of 20-30 min. This work represents a successful attempt to prepare functionalized monoliths via direct copolymerization of monomers with desired functionalities. Compared to earlier publications, additional Surface modifications were avoided and the PEGDA crosslinker helped to improve the biocompatibility of the monolithic backbone. (C) 2009 Elsevier B.V. All rights reserved.