A megaporous material harbouring a peptide ligand for affinity IgG purification

Area of Science:

• Biochemical Engineering
• Affinity Chromatography
• Protein Purification

Background:

• Protein A affinity chromatography is limited by high costs and ligand instability.
• Developing cost-effective and stable alternatives for IgG purification is crucial for biopharmaceutical manufacturing.

Purpose of the Study:

• To synthesize and evaluate a novel peptide-based adsorbent (MP-Pep) for IgG capture.
• To compare the performance of MP-Pep with Protein A chromatography.

Main Methods:

• Chemical synthesis of a short peptide ligand with IgG affinity.
• Immobilization of the peptide onto a megaporous cryogel support using thiol-epoxy click chemistry.
• Evaluation of static and dynamic binding capacities through adsorption isotherms and breakthrough analysis.

Main Results:

• MP-Pep exhibited a maximum static binding capacity of 30-60 mg/mL for therapeutic human IgG (ThIgG).
• Dynamic binding capacity was 9.0 mg/mL, comparable to the Protein A control (9.7 mg/mL).
• Cost-effective preparation and reasonable binding capacity were identified as key advantages.

Conclusions:

• MP-Pep represents a promising, economical alternative to Protein A for IgG purification.
• The adsorbent shows potential for bioprocessing, especially with high-concentration feedstocks due to cooperative binding effects.