Biolin Scientific Q-Sense QCM-D for understanding protein adsorption

Thursday, 01 July, 2021 | Supplied by: ATA Scientific Pty Ltd

Protein aggregates are a major challenge during pharmaceutical drug development that affects drug quality and safety. Biotherapeutics such as monoclonal antibodies (mAbs), frequently packaged at high concentration in syringes, can become unstable and form aggregates when they interact with the syringe surface coated with a lubricant like silicone oil. These aggregates have the potential to enhance immunogenicity and therefore need to be screened and controlled.

Understanding protein–surface interactions and how proteins adsorb at the silicone oil/water interface can help optimise formulation additives, such as stabilisers and surfactants, as well as the packaging used in the development and manufacture of new protein therapeutics.

Using Q-Sense QCM-D, a surface-sensitive technology that monitors mass uptake at the surface, the protein–silicone oil surface interaction can be analysed in real time. In addition to the mass, QCM-D also senses the structure of the layer adsorbed (or bound) at the surface. The adsorption behaviour of the protein, both in the absence and presence of different surfactants, can also be measured and compared.

In a recent study1, a group of researchers set out to study the surface activity of mAbs and whether two commonly used surfactants would lower their likelihood of adsorption and aggregation. Combining insights from the QCM-D analysis with information from complementary characterisation techniques, the study showed a direct relationship between mAbs adsorption at the oil–water interface and aggregation. The study also showed that surfactants, which will competitively adsorb to the interface, will lower the aggregation of the mAbs.

Reference: 1 Aadithya Kannan, Ian C. Shieh, Patrick G. Negulescu, Vineeth Chandran Suja, and Gerald G. Fuller; Adsorption and Aggregation of Monoclonal Antibodies at Silicone Oil–Water Interfaces; Mol. Pharmaceutics 2021, 18, 4, 1656–1665

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