Exploring the Unique Selectivity of Hydrophobic Cation Exchanger Nuvia cPrime for the Removal of a Major Process Impurity: A Case Study with IgM

Author(s): Xuemei M. He*, Carsten Voß, Jidong Li.

Journal Name: Current Protein & Peptide Science

Volume 20 , Issue 1 , 2019

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Abstract:

Background: Mixed-mode chromatography is becoming an important tool for downstream process purification, as it provides the selectivity and robustness unmatched by conventional singlemode chromatographic methods. The joint action of multiple functionalities present on the ligands of mixed-mode chromatography matrices effectively enhances the separation of target molecules from impurities.

Material and Methods: Using Nuvia cPrime as an example, we elucidate the separation principles of hydrophobic cation exchange mixed-mode chromatography and its difference from traditional strong cation exchangers. We have developed a Nuvia cPrime based polish purification step specifically for the removal of a major process contaminant, which has an isoelectric point similar to that of the target monoclonal IgM molecule. Additional purification was accomplished using a second mixed-mode chromatography column packed with Ceramic Hydroxyapatite.

Conclusion: The monoclonal IgM prepared with this new process fully retained its biological activity and was free of high molecular weight aggregates, a product quality that was not achievable in previous attempts using traditional ion exchange or hydrophobic interaction chromatography.

Keywords: Mixed-mode, protein purification, chromatography method development, hydrophobic cation exchange, IgM, selectivity, process impurity.

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Article Details

VOLUME: 20
ISSUE: 1
Year: 2019
Page: [65 - 74]
Pages: 10
DOI: 10.2174/1389203718666171017130506
Price: $58

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