Purification of antibody fragments via interaction with detergent micellar aggregates.

ABSTRACT: The research described in this report seeks to present proof-of-concept for a novel and robust platform for purification of antibody fragments and to define and optimize the controlling parameters. Purification of antigen-binding F(ab')₂ fragments is achieved in the absence of chromatographic media or specific ligands, rather by using clusters of non-ionic detergent (e.g. Tween-60, Brij-O20) micelles chelated via Fe²⁺ ions and the hydrophobic chelator, bathophenanthroline (batho). These aggregates, quantitatively capture the F(ab')₂ fragment in the absence or presence of E. coli lysate and allow extraction of only the F(ab')₂ domain at pH 3.8 without concomitant aggregate dissolution or coextraction of bacterial impurities. Process yields range f

SUBMITTER: Dhandapani G 

PROVIDER: S-EPMC8175343 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature