Purifying Antibodies


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Thursday, May 12

12:00 pm Registration


Purification Strategies 

1:30 Chairperson’s Opening Remarks

Judy Chou, Ph.D., Vice President, R&D, Tanvex Biologics, Inc.


» 1:40 Opening Keynote Presentation: 

Can the Antibody Purification Platform be Improved? 

Douglas Cecchini Douglas Cecchini, Ph.D., Director, Technical Development, Biogen Idec, Inc. 

In recent years, technological development for the purification of monoclonal antibodies and Fc fusion proteins has, to some extent, reached a plateau. However, new challenges posed by highly productive cell culture processes, the increasing demands on multi-product manufacturing facilities, and the Quality by Design initiative would benefit from further improvements to purification technologies. A number of innovative approaches that address these challenges will be presented. 

» 2:10 Featured Presentation: 

Purification of Antibody Fragments and Alternative Protein Scaffolds using the Strep-Tag, the His-Tag and Other Affinity Tags

Arne SkerraArne Skerra, Ph.D., Professor, Biological Chemistry, Technical University of Munich

The quick purification of recombinant proteins under standardized conditions is crucial for their functional optimization, in particular during biological drug discovery and development. While many affinity tags have been proposed over the years, only few offer the beneficial features of high purification efficiency, re-use of the affinity matrix, native elution and minimal interference with protein structure and function. A survey of established affinity tags and some case studies of Fab fragments, Anticalins and PASylated biologicals will be presented.

            Sponsored bySemba2:40 Continuous mAb Purification using Simulated Moving Bed: Taking the Chromatography Platform to the Next Level
Alla Zilberman, Ph.D., Director, Applications, Semba Biosciences, Inc.Chromatography as a bioprocessing platform has not kept pace with the demand for higher flexibility, higher productivity and lower costs in the purification of protein‐based pharmaceuticals. Continuous multicolumn protein separations through simulated moving bed chromatography elevate the chromatographic platform by conversion of the conventional batch process to a continuous process. Several purification methods including the “industry-standard” Protein A and size exclusion chromatography can be performed continuously on an automated bench top Octave™ Chromatography System. The results demonstrate more efficient use of chromatography media, reduced resin and buffer consumption, and higher throughput, making continuous chromatography an improved alternative to single column methods.  

2:55 Sponsored Presentation (Opportunity Available)

3:10 Refreshment Break in the Exhibit Hall with Poster Viewing

4:00 Options for the Production and Purification of Fab Antibody Fragments

Gavin Wild, Ph.D., Senior Scientist, Antibody Biology, UCB New Medicines

Antibody fragments such as Fab offer a structurally simply and physically robust format for therapeutic candidates.  The purification and subsequent conjugation of antibody fragments at scale bring several challenges which must be overcome.  A number of options for robust, efficient, and scalable processes have been developed by exploitation of the target molecule properties, combined with a range of chromatography matrices.  Downstream purification case studies covering the harvest/extraction, primary capture and subsequent polishing steps for Fab expressed in both mammalian and E.coli systems will be presented.

4:30 mAb Downstream Filtration Development: A Platform Approach for Variable Feed Streams

Bruno MarquesBruno Marques, Ph.D., Investigator, Biopharmaceutical Development, GlaxoSmithKline

In order to de-bottleneck high-producing monoclonal antibody (MAb) processes at the commercial scale, highly efficient, cost-effective, and predictable platform downstream unit operations are required. This paper presents the development of robust downstream filtration steps – employing depth, nano-, ultra-, and membrane filter technology – capable of scaling up to 20,000 L bioreactors with MAb titers of 3 g/L and above. By utilizing a statistical approach to experimental design, various filter fouling models, as well as high-throughput systems to alter buffer conditions, we were able to identify a combination of operating parameters and raw materials capable of processing MAbs with different biophysical properties, impurity profiles, and formulation requirements.

5:00 Close of Day

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