Peptide immobilized monolith containing tentacle-type functionalized polymer chains for high-capacity binding of immunoglobulin G

• A high-capacity and high-permeability monolith was prepared for IgG purification.
• Peptides immobilized tentacles provided the monolith with high IgG binding capacity.
• Macroporous channels endowed the monolith with high permeability for fast separation.
• Repeated separation tests proved that the monolith has excellent stability.
• The affinity tentacle monolith separated successfully IgG from diluted human blood sample.

A peptide immobilized tentacle-type monolith is developed here for high-performance IgG purification. In this work, the glucose-anchored GMA molecules serve as monomers to be grafted into the tentacle-type chains on highly porous monolith by a series of chemical reactions. While maintaining high column permeability, the tentacle grafting endows the monolith with lots of reactive handles to anchor more peptides. With that, the grafted monolith shows high peptide density of about 155 μmol mL−1, up to approximately 4.7 times higher over the ungrafted one (33 μmol mL−1). As a result, the static adsorbing capacity and dynamic adsorption capacity at 50% breakthrough point reach 101.8 and 83.3 mg mL−1 for IgG adsorption, respectively. Regeneration, recycle and reuse of grafted monolith are highly successful for 25 runs without obvious capacity loss. By taking these advantages of high capacity and excellent structure stability, the affinity grafted monolith is evaluated by using cleared human blood supernatant. And the result shows the peptide immobilized tentacle type monolith displays excellent specificity and high effectiveness for IgG purification.