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Related Experiment Video

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Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
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An Integrated Approach to Aggregate Control for Therapeutic Bispecific Antibodies Using an Improved Three Column Mab

Cassia Andrade1, Lindsay Arnold2, Dana Motabar1

  • 1Purification Process Sciences, MedImmune LLC, One MedImmune Way, Gaithersburg, Maryland, 20878.

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|October 10, 2018
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Summary

This study presents an improved purification process for bispecific antibodies (scFv-IgGs) with high aggregate levels. The optimized method significantly reduces aggregates, enhancing purification yield and robustness for therapeutic antibody production.

Keywords:
aggregate removalantibodiesbispecificpurification process

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Area of Science:

  • Biotechnology
  • Biochemical Engineering
  • Protein Purification

Background:

  • Single chain variable fragment-IgGs (scFv-IgGs) are bispecific antibodies prone to high aggregate formation (10%-30%) during mammalian cell culture.
  • High aggregate levels in scFv-IgGs reduce purification yields and challenge conventional monoclonal antibody (mAb) purification platforms, particularly cation exchange chromatography (CEX).

Purpose of the Study:

  • To develop and evaluate orthogonal methods for aggregate removal in scFv-IgG purification.
  • To improve the robustness and yield of a three-column purification process for high-aggregate scFv-IgGs.

Main Methods:

  • Bench-scale evaluation of Protein A chromatography with pH gradient elution, high-performance tangential flow filtration (HP-TFF), and calcium phosphate precipitation.
  • Pilot-scale validation of the most promising variants: Protein A pH gradient elution followed by calcium phosphate precipitation.

Main Results:

  • Protein A pH gradient elution and calcium phosphate precipitation effectively reduced aggregate burden prior to CEX.
  • Aggregate levels were reduced from 15%-23% to 2%-3% post-CEX.
  • The optimized process achieved an overall yield of 71%.

Conclusions:

  • An improved three-column purification process, incorporating Protein A gradient elution and/or calcium phosphate precipitation, is feasible for high-aggregate scFv-IgG bispecific antibodies.
  • This approach enhances purification robustness and monomer yield, addressing a key challenge in bispecific antibody manufacturing.