The Multi-Attribute Method (MAM), An Advanced LC-MS Approach for Protein A Resin Performance and Lifecycle Evaluation
Background: Protein A resins are indispensable for monoclonal antibody (mAb) production, yet their condition and performance are traditionally assessed using indirect or qualitative methods. In this study, the multi-attribute method (MAM), previously applied to therapeutic protein characterization, is systematically adapted for the first time as a unified liquid chromatography–mass spectrometry (LC-MS) platform for Protein A resin analysis. Method: Four Cytiva Protein A resins, MabSelect™, MabSelect SuRe™, MabSelect SuRe™ LX, and MabSelect™ PrismA, were evaluated by MAM for resin identity, Protein A ligand integrity, fouling by impurities, and cleaning performance. Results: MAM enables resin-specific peptide fingerprinting and quantitative monitoring of Protein A ligand post-translational modifications (PTMs), including deamidation, isomerization, and fragmentation induced by repeated clean-in-place (CIP) cycles. Comparative analysis of virgin and used resins revealed ligand degradation and fouling despite engineered alkaline stability, with MabSelect™ showing the greatest susceptibility. Importantly, residual monoclonal antibodies (mAbs) and host cell proteins (HCPs) were directly detected and quantified from the resin matrix, providing a molecular-level assessment of resin cleaning effectiveness not achievable with conventional approaches. Conclusions: This work establishes MAM as a novel, sensitive, and comprehensive strategy for Protein A resin lifecycle management, delivering actionable insight for resin selection, cleaning optimization, and downstream process development.
Authors
- Babita Saxena Parekh
- George Zhang (ORCID: https://orcid.org/0000-0003-2073-7109)
- Ming-Ching Hsieh
- Timothy Blanc
- Matthew Larsen
Institutions
- Eli Lilly (United States) (US)
Publication Details
- Journal
- Antibodies
- Published
- 2026-03-23
- DOI
- https://doi.org/10.3390/antib15020026
- Primary Topic
- Protein purification and stability
- Type
- article
- Field-Weighted Citation Impact
- 0.00