Novel Surfactant Compatibility with Downstream Protein Bioprocesses

Area of Science:

• Biotechnology
• Chemical Engineering
• Protein Chemistry

Background:

• Antibody downstream processing involves complex purification steps that can compromise product integrity.
• Protein aggregation and fouling of equipment are significant challenges during antibody manufacturing.

Purpose of the Study:

• To evaluate N-myristoyl phenylalanine polyether amine diamide (FM1000) as a process aid in antibody downstream processing.
• To assess FM1000's efficacy in preventing protein aggregation and surface fouling.
• To compare FM1000's performance and removal characteristics with traditional surfactants like polysorbates.

Main Methods:

• Investigated FM1000's ability to stabilize proteins against pumping-induced aggregation.
• Assessed FM1000's effectiveness in preventing antibody fouling on polymeric surfaces.
• Evaluated FM1000's removal via ultrafiltration/diafiltration and compared its chromatographic behavior to polysorbates.

Main Results:

• FM1000 effectively stabilized proteins against aggregation and prevented antibody fouling.
• FM1000 demonstrated tunable removal during buffer exchange steps.
• FM1000 exhibited faster and more predictable elution from purification units compared to polysorbates.

Conclusions:

• FM1000 is a versatile process aid for antibody downstream processing, enhancing product stability and preventing fouling.
• FM1000 offers advantages over traditional surfactants in terms of removal and purification efficiency.
• The tunable nature of FM1000 allows for tailored application in various downstream processing scenarios.