Detergent micelle conjugates containing amino acid monomers allow purification of human IgG near neutral pH

Gunasekaran Dhandapani, Ellen Wachtel, Guy Patchornik

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

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.
Original languageEnglish
Article number123358
JournalJournal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences
Volume1206
Early online date2022
DOIs
StatePublished - 15 Aug 2022

Keywords

  • Antibody purification
  • Protein A
  • Non-ionic surfactant micelles

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