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May 20, 2026European Journal of Biology0 citationsOpen Access

Design of Experiments–Driven Purification of Anti-Vascular Endothelial Growth Factor Monoclonal Antibodies

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YTYüksel TopaloğluMarmara UniversityÜŞÜlkü Yılmaz ŞahinAridis Pharmaceuticals (United States)AYAyşen YaratMarmara University

Key Points

  • The aim is to evaluate multimodal chromatography as a viable alternative to protein A chromatography for purifying anti-VEGF monoclonal antibodies.
  • Used PROchievA and mAbSelect PrismA for protein A purification and Capto MMC, Nuvia cPrime for multimodal purification.
  • Performed experiments based on designs created with Modde 13 software.
  • Analyzed data from purification experiments using the same software.
  • Protein A purification yielded 87.2%–93% while multimodal yielded 57.8%–65.2%.
  • Multimodal purification achieved approximately 10% greater removal of acidic and basic charge variants in a single step.
  • Higher purity mAbs were confirmed via sodium dodecyl sulphate–polyacrylamide gel electrophoresis.

Abstract

Objective: This study demonstrated the successful application of multimodal chromatography (MMC) as an alternative to protein A chromatography for the purification of mAbs with anti-vascular endothelial growth factor properties.Materials and Methods: PROchievA and mAbSelect PrismA resins were used for protein A chromatographic purification, while Capto MMC and Nuvia cPrime resins were used for multimodal chromatographic purification. Each purification study was conducted as the initial capture step for the mAb produced in the Chinese hamster ovary cell culture. The experimental designs for the purification steps were developed using Modde 13 software, and the resulting data were analysed with the assistance of the same software.Results: Purification steps using protein A resins resulted in yields of approximately 87.2%–93%, whereas yields obtained with multimodal resins were approximately 57.8%–65.2%. The multimodal purification step enabled the production of a monoclonal antibody (mAb) with a higher purity compared to the protein A purification step. It also showed superior performance compared to protein A resins in the removal of acidic and basic variants, achieving approximately 10% greater reduction of these variants in a single step and enabling the production of a purer mAb product.Conclusion: This study highlighted the potential of MMC to enhance the purity of mAbs with greater efficiency in removing charge variants. The purified mAbs were confirmed based on their mass values using the sodium dodecyl sulphate–polyacrylamide gel electrophoresis.

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Cite This Study

Topaloğlu et al. (2026) studied this question.

synapsesocial.com/papers/6a0d5114f03e14405aa9d5f2https://doi.org/10.26650/eurjbiol.2026.1842218
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