Investigation of alkaline effects on Protein A affinity ligands and resins using high resolution mass spectrometry

Wetterhall, Magnus; Ander, Mats; Björkman, Tomas; Musunuri, Sravani; Palmgren, Ronnie; Rodrigo, Gustav

doi:10.1016/j.jchromb.2020.122473

Cited by 3 publications

(1 citation statement)

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“…Moreover, by optimizing the cleaning and resin regeneration protocols, the lifetime of MabSelect SuRe™ could be prolonged up to 150 cycles, which may translate into economical savings in large-scale production ( Zhou et al, 2019 ). Recently, new resin with protein A ligand designed by protein engineering (MabSelect TM PrismA) showed greater stability for regeneration process ( Wetterhall et al, 2021 ), however, this chromatographic material has not been reported to purify Fc-fusion proteins.…”

Section: Fc-fusionmentioning

confidence: 99%

Purification of Modified Therapeutic Proteins Available on the Market: An Analysis of Chromatography-Based Strategies

Sánchez‐Trasviña

Flores-Gatica

Enriquez-Ochoa

et al. 2021

Front. Bioeng. Biotechnol.

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Proteins, which have inherent biorecognition properties, have long been used as therapeutic agents for the treatment of a wide variety of clinical indications. Protein modification through covalent attachment to different moieties improves the therapeutic’s pharmacokinetic properties, affinity, stability, confers protection against proteolytic degradation, and increases circulation half-life. Nowadays, several modified therapeutic proteins, including PEGylated, Fc-fused, lipidated, albumin-fused, and glycosylated proteins have obtained regulatory approval for commercialization. During its manufacturing, the purification steps of the therapeutic agent are decisive to ensure the quality, effectiveness, potency, and safety of the final product. Due to the robustness, selectivity, and high resolution of chromatographic methods, these are recognized as the gold standard in the downstream processing of therapeutic proteins. Moreover, depending on the modification strategy, the protein will suffer different physicochemical changes, which must be considered to define a purification approach. This review aims to deeply analyze the purification methods employed for modified therapeutic proteins that are currently available on the market, to understand why the selected strategies were successful. Emphasis is placed on chromatographic methods since they govern the purification processes within the pharmaceutical industry. Furthermore, to discuss how the modification type strongly influences the purification strategy, the purification processes of three different modified versions of coagulation factor IX are contrasted.

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Section: Fc-fusionmentioning

confidence: 99%