Capto� MMC is a mixed-mode chromatographic adsorbent that is functionalized with a ligand carrying both a hydrophobic and an electrostatic group. The dual functionality makes optimization of conditions for binding and elution more challenging. Better understanding of the interaction between proteins and the mixed-mode adsorbent is needed in order to facilitate rapid development/evaluation of a chromatographic step utilizing the unique properties of the adsorbent. Thermodynamic modeling of protein adsorption on Capto MMC is done by utilizing established adsorption isotherm. Data are obtained through automated robotic high-throughput screening in 96-well microtitre plates and show the effect of salt concentration and pH, and influence of the ligand hydrophobicity under the different conditions, on the interaction of model proteins and a monoclonal antibody with Capto MMC. In addition, experimental designs based on adsorption isotherm models and designs used in standard DoE studies are compared and their applicability in studies describing adsorption equilibria are discussed.

Mechanism of interaction between proteins and the mixed-mode adsorbent, Capto MMC

243rd National Meeting (2012)

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