ArticlemAbs
Purification of monoclonal antibodies by hydrophobic interaction chromatography under no-salt conditions.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Multimodal Anion-Exchange Resins for Chromatographic Separation of Antibody Aggregates.Biomolecules · 2026Article
- The Production and Purification of Therapeutic Antibodies: A Comprehensive Analysis of Process- and Product-Related Contaminants.Biomolecules · 2026Review
- Removal of Aggregates During Bispecific Antibody Purification Using Hydrophobic Interaction Chromatography.Membranes · 2025Article
- Antibody Aggregate Removal by Multimodal Chromatography.Molecules (Basel, Switzerland) · 2025Review
- Purification of Monoclonal Antibodies Using Chromatographic Methods: Increasing Purity and Recovery.Advanced pharmaceutical bulletin · 2025Review
- Biopharmaceutical Analysis by HPLC: Practices and Challenges.Chonnam medical journal · 2025Article
- Modeling the behavior of monoclonal antibodies on hydrophobic interaction chromatography resins.Bioresources and bioprocessing · 2024Article
- Challenges and solutions for the downstream purification of therapeutic proteins.Antibody therapeutics · 2024Review
- Microbial lipases and their industrial applications: a comprehensive review.Microbial cell factories · 2020Review
- A Purification Strategy Utilizing Hydrophobic Interaction Chromatography to Obtain Homogeneous Species from a Site-Specific Antibody Drug Conjugate Produced by AJICAP™ First Generation.Antibodies (Basel, Switzerland) · 2020Article
- The uniqueness of flow in probing the aggregation behavior of clinically relevant antibodies.Engineering reports : open access · 2020Article
- An Integrated Approach to Aggregate Control for Therapeutic Bispecific Antibodies Using an Improved Three Column Mab Platform-Like Purification Process.Biotechnology progress · 2019Article
- Evolving trends in mAb production processes.Bioengineering & translational medicine · 2017Review
- Pool-less processing to streamline downstream purification of monoclonal antibodies.Engineering in life sciences · 2017Article
- Different Stationary Phase Selectivities and Morphologies for Intact Protein Separations.Chromatographia · 2017Review
- Dystrophin hydrophobic regions in the pathogenesis of Duchenne and Becker muscular dystrophies.Bosnian journal of basic medical sciences · 2015Article
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- Strategies for removing two "problematic" host cell proteins, using an "end-to-end" approach.Biotechnology progressArticle
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrophobic interaction chromatography (HIC) is commonly used as a polishing step in monoclonal antibody purification processes. HIC offers an orthogonal selectivity to ion exchange chromatography and can be an effective step for aggregate clearance and host cell protein reduction. HIC, however, suffers from the limitation of use of high concentrations of kosmotropic salts to achieve the desired separation. These salts often pose a disposal concern in manufacturing facilities and at times can cause precipitation of the product. Here, we report an unconventional way of operating HIC in the flowthrough (FT) mode with no kosmotropic salt in the mobile phase. A very hydrophobic resin is selected as the stationary phase and the pH of the mobile phase is modulated to achieve the required selectivity. Under the pH conditions tested (pH 6.0 and below), antibodies typically become positively charged, which has an effect on its polarity and overall surface hydrophobicity. Optimum pH conditions were chosen under which the antibody product of interest flowed through while impurities such as aggregates and host cell proteins bound to the column. This strategy was tested with a panel of antibodies with varying pI and surface hydrophobicity. Performance was comparable to that observed using conventional HIC conditions with high salt.
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