Purification of IgG's, IgM's and Human Serum Albumin with: Engineered-Micelles

Guy Patchornik, Chemical Sciences , Ariel University, Ariel, Israel (guyp@ariel.ac.il)

We introduce a new concept and a potentially general platform for antibody (Ab) purification that does not rely on chromatography nor specific ligands; rather, makes use of detergent aggregates capable of efficiently capturing Ab's while rejecting hydrophilic impurities. Captured Ab's are extracted from the aggregates in pure form (>95%, by SDS-PAGE) without aggregate dissolution.

The aggregates studied consist of conjugated "Engineered-micelles" built from nonionic detergents (e.g., Tween or Brij), the hydrophobic chelator, bathophenanthroline and Fe²⁺ ions. When tested in serum-free media, IgG’s (at 25 mg\ml) and IgM's (at 1.5 mg\ml) are recovered in high yields (93-98%) while preserving their structure (by CD), specificity (by ELISA) and mono-dispersity (by CD). Antibody capture and extraction are both performed at close to neutrality. Similar findings are found with human serum albumin (HSA). Possible integration of the approach within industrial-scale, downstream processing of therapeutic monoclonal Ab's and plasma fractionation, will be discussed.