Industrial scale production of therapeutic monoclonal antibodies (mAbs) is commonly achieved with Protein A chromatography, a process that requires exposure of the antibody to strongly acidic conditions during the eluting step. Exposure to acid inactivates virus contaminants but may, in parallel, lead to antibody aggregation that must be eliminated or kept at acceptably low levels. This report seeks to provide a practical method for overcoming a long-standing problem. We show how Brij-O20 detergent micelles, conjugated by the amphiphilic [(bathophenanthroline)₃:Fe²⁺] complex in the presence of amino acid monomers: phenylalanine (Phe), tyrosine (Tyr), tryptophan (Trp), isoleucine (Ile) or valine (Val), efficiently capture polyclonal human IgG (hIgG) at neutral pH and allow its recovery by extraction either at pH 4 (85–97% yield) or at pH 6.3 (72–84% yield). Of the five amino acid monomers surveyed, Phe or Tyr produced the highest overall process yield at both pH 4 and 6.3. The monomeric state of the purified hIgG's was confirmed by dynamic light scattering (DLS). Potential advantages of the purification method are discussed.

治疗性单克隆抗体 (mAb) 的工业规模生产通常通过蛋白 A 色谱法实现，该过程需要在洗脱步骤中将抗体暴露于强酸性条件下。暴露于酸会使病毒污染物失活，但同时可能导致必须消除或保持在可接受的低水平的抗体聚集。本报告旨在为克服一个长期存在的问题提供一种实用的方法。我们展示了 Brij-O20 洗涤剂胶束如何与两亲性 [(bathophenanthroline) ₃ :Fe ^2+共轭] 在氨基酸单体存在下形成复合物：苯丙氨酸 (Phe)、酪氨酸 (Tyr)、色氨酸 (Trp)、异亮氨酸 (Ile) 或缬氨酸 (Val)，在中性 pH 条件下有效捕获多克隆人 IgG (hIgG) 并使其恢复通过在 pH 4（产率 85-97%）或 pH 6.3（产率 72-84%）下提取。在所调查的五种氨基酸单体中，Phe 或 Tyr 在 pH 4 和 6.3 时产生最高的总工艺收率。通过动态光散射 (DLS) 确认纯化的 hIgG 的单体状态。讨论了纯化方法的潜在优势。