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

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


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 Fe 2+ 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.

Original languageEnglish
Pages (from-to)583-592
Number of pages10
Issue number3
StatePublished - 3 Apr 2019


  • Antibody purification
  • Chromatography
  • IgG
  • Protein A
  • Protein G


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