1. CaptureSelect FcXP affinity medium exhibits strong aggregate separation capability.
- Author
-
Dong W, Zhang D, and Li Y
- Subjects
- Recombinant Fusion Proteins chemistry, Recombinant Fusion Proteins isolation & purification, Recombinant Fusion Proteins genetics, Protein Aggregates, Humans, Immunoglobulin Fc Fragments chemistry, Immunoglobulin Fc Fragments isolation & purification, Chromatography, Affinity methods, Antibodies, Bispecific chemistry, Antibodies, Bispecific isolation & purification, Staphylococcal Protein A chemistry
- Abstract
Protein A affinity chromatography has been widely used for initial product capture in recombinant antibody/Fc-fusion purification. However, in general Protein A lacks the capability of separating aggregates (unless the aggregates are too large to enter the pores of resin beads or have their Protein A binding sites buried, in which case the aggregates do not bind). In the current work, we demonstrated that CaptureSelect FcXP affinity medium exhibited strong aggregate separation capability and effectively removed aggregates under pH or conductivity gradient elution in two bispecific antibody (bsAb) cases. For these two cases, aggregate contents were reduced from >16% and >22% (in the feed) to <1% and <5% (in the eluate) for the first and second bsAbs, respectively. While more case studies are required to further demonstrate FcXP's superiority in aggregate removal, findings from the current study suggest that FcXP can potentially be a better alternative than Protein A for product capture in cases where aggregate content is high., (Copyright © 2024 Elsevier Inc. All rights reserved.)
- Published
- 2024
- Full Text
- View/download PDF