Iminodiacetic acid (IDA) is one of the chelating ligands most frequently employed in immobilized metal-ion affinity chromatography (IMAC) due to its ability to act as electron-pair donor, forming stable complexes with intermediate and borderline Lewis metal ions (electron acceptor). Thus, IDA can also be employed in ion exchange chromatography to purify positively charged proteins at neutral pH values. This study aimed to evaluate IDA as an ionogenic group (ion exchanger) immobilized on poly (ethylene vinyl alcohol) (PEVA) hollow fiber membranes for immunoglobulin G1 (IgG1) monoclonal antibody (MAb) purification. IDA-PEVA membranes showed considerable promise for MAb purification, since IgG1 was recovered in eluted fractions with traces of contaminants as confirmed by Western blotting and ELISA analysis. Quantification of IgG1 showed that a purity of 94.2% was reached in the elution step. Breakthrough curve and batch adsorption experiments showed that the MAb dynamic binding capacity (DBC) of 3.10 mg g-1 and the maximum adsorption capacity of 70 mg g-1 were of the same order of magnitude as those found in the literature. The results obtained showed that the IDA-PEVA hollow fiber membrane could be a powerful adsorbent for integrating large-scale processes for purification of MAb from cell culture supernatant.

中文翻译：

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通过膜色谱法评估亚氨基二乙酸（IDA）作为离子源基团对IgG1单克隆抗体的吸附。

亚氨基二乙酸（IDA）是固定化金属离子亲和色谱（IMAC）中最常用的螯合配体之一，因为它具有充当电子对供体的能力，可与中间和临界路易斯金属离子（电子受体）形成稳定的络合物。因此，IDA也可用于离子交换色谱中，以在中性pH值下纯化带正电荷的蛋白质。这项研究旨在评估IDA作为固定在聚（乙烯乙烯醇）（PEVA）中空纤维膜上的离子源基团（离子交换剂），用于纯化免疫球蛋白G1（IgG1）单克隆抗体（MAb）。IDA-PEVA膜显示出可用于单抗纯化的巨大前景，因为通过蛋白质印迹和ELISA分析证实，IgG1可以洗脱部分中的痕量污染物回收到IgG1中。IgG1的定量显示洗脱步骤的纯度达到94.2％。突破曲线和分批吸附实验表明，3.10 mg g-1的MAb动态结合能力（DBC）和70 mg g-1的最大吸附能力与文献中发现的数量级相同。所得结果表明，IDA-PEVA中空纤维膜可能是整合大规模从细胞培养上清液中纯化MAb的强大吸附剂。