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Optimizing high throughput antibody purification by using continuous chromatography media.

Identifieur interne : 000812 ( Main/Exploration ); précédent : 000811; suivant : 000813

Optimizing high throughput antibody purification by using continuous chromatography media.

Auteurs : Rebecca E. Butcher [Australie] ; Genevieve Martin-Roussety [Australie] ; Rebecca A. Bradford [Australie] ; Andrea Tester [Australie] ; Catherine Owczarek [Australie] ; Matthew P. Hardy [Australie] ; Chao-Guang Chen [Australie] ; Georgina Sansome [Australie] ; Louis J. Fabri [Australie] ; Peter M. Schmidt [Allemagne]

Source :

RBID : pubmed:30917921

Descripteurs français

English descriptors

Abstract

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.

DOI: 10.1016/j.pep.2019.03.011
PubMed: 30917921


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

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<term>Chromatography, Affinity (MeSH)</term>
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<div type="abstract" xml:lang="en">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.</div>
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