Compression and protein-protein interactions as triggers for aggregation of monoclonal antibodies at interfaces
July 14-17, 2019
Aggregation of biopharmaceuticals triggered by interfaces is a challenge at various levels from upstream processing to patient application. We specifically investigated the air-liquid interface. A combination of Langmuir-Blodgett Trough experiments, Infrared Reflection-Absorption Spectroscopy, Brewster Angle Microscopy, Atomic Force Microscopy and Profile Analysis Tensiometry could demonstrate that the film formed by monoclonal antibodies (mabs) at the interface can be substantially condensed upon compression due to interface movement. Protein-protein interactions subsequently are a key element which determines whether large aggregates result from this phase upon decompression.
Thus, not only addition of surface active molecules is a remedy to solve the problem of surface induced aggregation. Additionally, factors which strongly affect the protein-protein interactions, specifically pH and ionic strength are starting points.
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Inas Elbialy, Wolfgang Friess, and Ellen Koepf, "Compression and protein-protein interactions as triggers for aggregation of monoclonal antibodies at interfaces" in "Biological and Pharmaceutical Complex Fluids III: Protein Self-Assembly, Rheology and Interfacial Properties", Samiul Amin, Manhattan College, USA Miguel Rodrigues, University of Lisbon, Portugal Paolo Arosio, ETHZ, Switzerland Eds, ECI Symposium Series, (2019). https://dc.engconfintl.org/bpcf_iii/9