Inhibited fragmentation of mAbs in buffered ionic liquids

Area of Science:

• Biochemistry
• Materials Science
• Chemical Engineering

Background:

• Monoclonal antibodies (mAbs) are crucial therapeutics but require stable storage and transport conditions.
• Maintaining the structural and functional integrity of antibodies like epidermal growth factor receptor monoclonal antibody (EGFR mAb) is critical for efficacy.
• Current biological buffers face limitations in preserving antibody stability under various conditions.

Purpose of the Study:

• To investigate the efficacy of choline-based buffered ionic liquids (BILs) as novel biological buffers.
• To evaluate the impact of BILs on the biological, structural, and chemical stability of EGFR mAb.
• To assess the potential of BILs as green alternatives for antibody storage and transportation.

Main Methods:

• EGFR mAb was incubated in various choline-based BIL formulations.
• Biological stability was assessed through functional assays.
• Structural integrity was analyzed using techniques like circular dichroism.
• Chemical stability was monitored using methods such as size exclusion chromatography.

Main Results:

• Substantially enhanced biological, structural, and chemical stability of EGFR mAb was observed in the tested BILs.
• BILs demonstrated superior performance compared to conventional buffers in preserving antibody integrity.
• No significant aggregation or degradation of EGFR mAb was detected in the optimized BIL formulations.

Conclusions:

• Choline-based BILs offer a promising new platform for stabilizing therapeutic antibodies.
• These green ionic liquids present a viable solution for enhancing antibody storage and transportation logistics.
• Further research into BILs could revolutionize biopharmaceutical formulation and delivery.