Biopurification of monoclonal antibody (mAb) through crystallisation
| Autor: | Siti S. Ramli, Frederik J. Link, Jinbo Ouyang, Ian Rosbottom, Jerry Y. Y. Heng, Wenqian Chen, Mingxia Guo, Xiaoyu Li |
|---|---|
| Přispěvatelé: | Engineering & Physical Science Research Council (EPSRC) |
| Rok vydání: | 2021 |
| Předmět: |
medicine.drug_class
Chemistry Critical factors 0904 Chemical Engineering Filtration and Separation 02 engineering and technology Chemical Engineering 021001 nanoscience & nanotechnology Monoclonal antibody Analytical Chemistry 020401 chemical engineering Biochemistry medicine 0204 chemical engineering 0210 nano-technology 0301 Analytical Chemistry |
| Zdroj: | Separation and Purification Technology. 263:118358 |
| ISSN: | 1383-5866 |
| DOI: | 10.1016/j.seppur.2021.118358 |
| Popis: | Therapeutics based on monoclonal antibody (mAb) represent the most advanced biopharmaceuticals, being able to treat a wide range of challenging diseases such as cancers and arthritis. As the scale of mAb production steadily increases with the demand for mAb-based therapeutics, the downstream biopurification continues to experience significant bottleneck due to the throughput limited nature of the current purification technology. Over the last decades, significant advances have been made in protein (and especially mAb) crystallisation as an alternative biopurification technology that offers high product stability and purity as well as scalability. This review starts with the discussion of general physicochemical properties of mAb before moving on to the in-depth discussion of the distinct phase behaviour of mAb in comparison with conventional globular proteins such as lysozyme. The final part of this review presents a summary of successful demonstrations of crystallisation scale-ups of mAb and discusses the critical factors (i.e. mixing and temperature control) to be considered. |
| Databáze: | OpenAIRE |
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