ArticlemAbs
Controlled conductivity at low pH in Protein L chromatography enables separation of bispecific and other antibody formats by their binding valency.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Rapid affinity-based purification of multi-specific antibodies using Kappa Select and Protein L.mAbs · 2025Article
- A two-column process for bispecific antibody purification based on MabSelect VL resin's strong byproduct removal capability.Journal of biological methods · 2025Article
- Advantages of MabSelect VH3, a novel VH3-specific Protein A resin, over its two conventional counterparts in purifying a VHH-based trispecific antibody.Journal of biological methods · 2025Article
- CH1-specific affinity resins possess the potential of separating heterodimer from homodimers in asymmetric bispecific antibody purification.Journal of biological methods · 2024Article
- Calcium chloride and arginine show diametrically opposite effects on antibody elution in Protein A and Protein L chromatography.Journal of biological methods · 2024Article
- Current trends and challenges in the downstream purification of bispecific antibodies.Antibody therapeutics · 2021Review
- Modelling of pH-dependence to develop a strategy for stabilising mAbs at acidic steps in production.Computational and structural biotechnology journal · 2020Review
- Article
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Authors and funding
11 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The complex molecular formats of recent therapeutic antibodies, including bispecific antibodies, antibody fragments, and other fusion proteins, makes the task of purifying the desired molecules in a limited number of purification steps more and more challenging. Manufacturing these complicated biologics can be substantially improved in the affinity capture stage if the simple bind-and-elute mode is accompanied by targeted removal of the impurities, such as mis-paired antibodies and oligomers or aggregates. Here, we report a method, based on the binding valency to Protein L resin, of separating proteins during the elution step by simply controlling the conductivity at low pH. We show that the method efficiently separated targeted antibodies from mis-paired and aggregated species. Notably, the number of Protein L binding sites can be built into the molecule by design to facilitate the purification. This method may be useful for purifying various antibody formats at laboratory and manufacturing scales.
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