Capture of antibodies in biopharmaceutical processes is most commonly performed using affinity chromatography on Protein A. While Protein A works well, the commercially available chromatography resin is expensive and its use requires testing of the bulk drug substance for residual Protein A leached from the chromatography column during operation. There has been interest for a long time in bulk phase methods, such as two-phase liquid extraction, as a lower cost alternative for antibody capture. Now a new bulk phase extraction method that appears to offer high purity for immunoglobulins has been reported.
A group led by Guy Patchornik from Ariel University in Israel investigated the ability to use engineered micelles, or detergent aggregates, made of Tween 20, a hydrophobic metal chelator and Fe2+ ions, to efficiently capture immunoglobulins from cell culture medium. Their findings demonstrate the ability to purify human and mouse IgG antibodies with 70-80% yield from serum-free medium while preserving their secondary structure. This platform is an intriguing antibody purification strategy, and the authors suggest that it could potentially replace Protein A column purification. The article, “A general platform for antibody purification utilizing engineered-micelles,” is authored by Gunasekaran Dhandapani, Assaf Howard, Thien Van Truong, Thekke V. Baiju, Ellina Kesselman, Noga Friedman, Ellen Wachtel, Mordechai Sheves, Dganit Danino, Irishi N. N. Namboothiri & Guy Patchornik and appears in mAbs 2019, vol 11(3), 583-592. DOI: 10.1080/19420862.2019.1565749.
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