(595b) Comparison of Protein Particle Formation in IgG1 Mabs Formulated with PS20 Vs. PS80 When Subjected to Interfacial Dilatational Stress

Polysorbates 20 and 80 are used in the formulation and development of protein therapeutics to mitigate the formation of protein particles when exposed to a variety of mechanical stresses. However, the efficiency of PS20 vs. PS80 in mitigating protein particle formation is debated. Here, we used a Langmuir trough to apply interfacial dilatational stress to IgG molecules (mAb1 and mAb2) that were formulated with either PS20 or PS80. Comparisons of the interfacial properties of these formulations, both in the absence and presence of interfacial stresses was correlated with protein particle formation data obtained using Micro-flow imaging (MFI). Our data shows that mAb1 formulated in PS20 demonstrates faster adsorption kinetics and higher surface activity than mAb1 formulated in PS80. When subjected to interfacial dilatational stresses, mAb1 formulated in PS20 is able to remain at the interface, while our compression/expansion data suggests that during multiple compression/expansion cycles, mAb1 replaces PS80 from the interface. Further, protein particle analysis of the interface and the bulk solution confirms that PS20 is much more effective at mitigating the formation of larger particles in the bulk and at the interface. This study continues to highlight the importance of interfacial analysis in the development and formulation of protein therapeutics in the biotechnology industry.