Optimizing high throughput antibody purification by using continuous chromatography media.

Autor: Butcher RE; CSL Limited, BIO21 Institute, 30 Flemington Road, Parkville, Victoria, 3010, Australia., Martin-Roussety G; CSL Limited, BIO21 Institute, 30 Flemington Road, Parkville, Victoria, 3010, Australia., Bradford RA; CSL Limited, BIO21 Institute, 30 Flemington Road, Parkville, Victoria, 3010, Australia., Tester A; CSL Limited, BIO21 Institute, 30 Flemington Road, Parkville, Victoria, 3010, Australia., Owczarek C; CSL Limited, BIO21 Institute, 30 Flemington Road, Parkville, Victoria, 3010, Australia., Hardy MP; CSL Limited, BIO21 Institute, 30 Flemington Road, Parkville, Victoria, 3010, Australia., Chen CG; CSL Limited, BIO21 Institute, 30 Flemington Road, Parkville, Victoria, 3010, Australia., Sansome G; CSL Limited, BIO21 Institute, 30 Flemington Road, Parkville, Victoria, 3010, Australia., Fabri LJ; CSL Limited, 45 Poplar Road, Parkville, Victoria, 3010, Australia., Schmidt PM; CSL Limited, BIO21 Institute, 30 Flemington Road, Parkville, Victoria, 3010, Australia; CSL Behring GmbH, R&D, Emil-von-Behring Str. 76, Marburg, 35041, Germany. Electronic address: Peter.Schmidt@cslbehring.com.
Jazyk: angličtina
Zdroj: Protein expression and purification [Protein Expr Purif] 2019 Jul; Vol. 159, pp. 75-82. Date of Electronic Publication: 2019 Mar 25.
DOI: 10.1016/j.pep.2019.03.011
Abstrakt: The ability to engineer monoclonal antibodies (mAbs) with high specificity made mAbs the fastest growing segment in the drug market. mAbs represent 8 of the top 20 selling drugs with combined sales of more than 57 billion US$ per year. The ability to purify large numbers of mAbs with sufficient yields for initial screening campaigns has direct impact on the timelines of a project. Automated liquid handling (ALH)-based mAb purification platforms have been used to facilitate the production of large numbers of mAbs. However, the ongoing pressure to de-risk potential lead molecules at an early development stage by including bio-physical characterization of mAbs has further increased the demand to produce sufficient quantities from limited sample volumes. A bottleneck so far has been the limited dynamic binding capacity of these systems, which is partly due to the binding properties of commonly used Protein A affinity matrices. The present publication suggests that by using a Protein A matrix optimized for continuous chromatography applications the yields of ALH-based but also standard lab-scale mAb purifications can be significantly increased without the need to change established protocols.
(Copyright © 2019 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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