Surface and Sefl-Associaciation Interaction of Proteins Characterized by QCM-D

A. Jaiswal, M. Poggi
Biolin Scientific, Inc., US

Keywords: QCM-D, proteins aggreegation, silicon oil


As proteins become important therapeutic agents in treating diseases, the storage and delivery of these drugs faces ever increasing challenges. Proteins tend to interact with surfaces of such storage and delivery device due to their amphiphilic nature, which may lead to the formation of aggregate. Particularly, their interaction with a syringe lubricant (silicone oil) has been shown to adversely affect formulations. Protein-surface adsorption and aggregation can adversely affect therapeutic protein development, manufacturing and formulation. Therefore, it is critical to understand and be able to measure these properties. The surface-sensitive technique Quartz Crystal Microbalance with Dissipation (QCM-D) allows quantification of the mass and viscoelasticity of protein layers adsorbed and aggregated on surfaces. Two studies demonstrate the utility of QCM-D to assess protein-surface interactions and aggregation, and determine concentrations and excipients that minimize these interactions. (1) The interaction of the therapeutic protein Abatacept with silicon oil at two concentrations and in the presence of the excipients Polysorbate-80 and Poloxamer 188. (2) The adsorption of two monoclonal antibodies (mAb1, mAb2) to silicon dioxide, polystyrene, Teflon and gold surfaces at two concentrations and in the presence of the excipient Polysorbate-80.