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A General Platform for Antibody Purification Utilizing Engineered-Micelles

A General Platform for Antibody Purification Utilizing Engineered-Micelles

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

MAbs. 2019 Apr;11(3):583-592.

PMID: 30618334

Abstract:

We introduce a new concept and potentially general platform for antibody (Ab) purification that does not rely on chromatography or specific ligands (e.g., Protein A); rather, it makes use of detergent aggregates capable of efficiently capturing Ab while rejecting hydrophilic impurities. Captured Ab are then extracted from the aggregates in pure form without co-extraction of hydrophobic impurities or aggregate dissolution. The aggregates studied consist of conjugated "Engineered-micelles" built from the nonionic detergent, Tween-20; bathophenanthroline, a hydrophobic metal chelator, and Fe2+ions. When tested in serum-free media with or without bovine serum albumin as additive, human or mouse IgGs were recovered with good overall yields (70-80%, by densitometry). Extraction of IgGs with 7 different buffers at pH 3.8 sheds light on possible interactions between captured Ab and their surrounding detergent matrix that lead to purity very similar to that obtained via Protein A or Protein G resins. Extracted Ab preserve their secondary structure, specificity and monomeric character as determined by circular dichroism, enzyme-linked immunosorbent assay and dynamic light scattering, respectively.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP1662017	Bathophenanthroline		1662-01-7	Price

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