An Affinity Complex Titration Isotherm for Mechanistic Modeling in Protein A Chromatography

A pH-dependent affinity complex titration isotherm is derived based on the stoichiometry of target binding and both target and ligand titration equilibria to facilitate mechanistic modeling for protein A chromatography. The final isotherm can be regarded as a direct modification of the Langmuir isotherm with an apparent capacity and equilibrium constant. The model parameters can be estimated from four elution experiments and the same model parameters can be extrapolated to a wide range of situations with accurate chromatogram predictions. The isotherm is shown to be compatible with different mAbs, resins, residence times, wash and elution buffer pHs, gradient lengths from 0 to 30 column volumes and column dimensions. The separation of a mAb mixture is presented as a case study.

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Publication Details

Journal
Biotechnology and Bioengineering
Published
2025-06-11
DOI
https://doi.org/10.1002/bit.29035
Citations
1
Primary Topic
Protein purification and stability
Type
article
Field-Weighted Citation Impact
0.81
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article

An Affinity Complex Titration Isotherm for Mechanistic Modeling in Protein A Chromatography

Todd M. Przybycien, Wendi Zhang, Virginia Lane DiNenna
1 citations
Biotechnology and Bioengineering
Protein purification and stability
0.81
article

An Affinity Complex Titration Isotherm for Mechanistic Modeling in Protein A Chromatography

Todd M. Przybycien, Wendi Zhang, Virginia Lane DiNenna
article en
1 citations

Abstract

A pH-dependent affinity complex titration isotherm is derived based on the stoichiometry of target binding and both target and ligand titration equilibria to facilitate mechanistic modeling for protein A chromatography. The final isotherm can be regarded as a direct modification of the Langmuir isotherm with an apparent capacity and equilibrium constant. The model parameters can be estimated from four elution experiments and the same model parameters can be extrapolated to a wide range of situations with accurate chromatogram predictions. The isotherm is shown to be compatible with different mAbs, resins, residence times, wash and elution buffer pHs, gradient lengths from 0 to 30 column volumes and column dimensions. The separation of a mAb mixture is presented as a case study.

Biotechnology and BioengineeringVol. 122(9)
Rensselaer Polytechnic Institute (US), Carnegie Mellon University (US)
Openalex Percentile: Top 27%
Protein purification and stability
0.81
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