Dhandapani, Gunasekaran ; Howard, Assaf ; Truong, Thien Van ; Baiju, Thekke V. ; Kesselman, Ellina ; Friedman, Noga ; Wachtel, Ellen ; Sheves, Mordechai ; Danino, Dganit ; Namboothiri, Irishi N. N. ; Patchornik, Guy (2019) A general platform for antibody purification utilizing engineered-micelles mAbs, 11 (3). pp. 583-592. ISSN 1942-0862
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Official URL: http://doi.org/10.1080/19420862.2019.1565749
Related URL: http://dx.doi.org/10.1080/19420862.2019.1565749
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 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.
Item Type: | Article |
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Source: | Copyright of this article belongs to Informa UK Limited. |
ID Code: | 121314 |
Deposited On: | 14 Jul 2021 09:16 |
Last Modified: | 14 Jul 2021 09:16 |
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