The current challenges faced in the formulation of high concentration protein-based therapeutics include protein stability, protein aggregation, and high viscosity. Although there has been significant progress in developing a mechanistic understanding of the protein systems themselves, the impact of other formulation components has been limited. Excipients like surfactants such as Polysorbates, or Poloxamers which are commonly utilized in bio-therapeutic formulations may potentially impact many of these aspects. This systematic study details the effect of these excipients on protein aggregation and corresponding effects on bulk and surface rheology evolution. Additionally, the impact on interfacial and surface properties has been limited in the range of formulation conditions and impacts on interfacial rheology have not been investigated in detail. In this study, we utilize a range of advanced characterization techniques such as surface/ interfacial rheometry, tensiometry, dynamic light scattering, as well as thermal aggregation studies to develop new insights into the impact of surfactants i.e. polysorbate 20, polysorbate 80 and poloxamer P188 on the aggregation behavior, rheology and interfacial and surface properties of Bovine Serum Albumin (BSA) and lysozyme.<b> </b>In conclusion, competitive adsorption between proteins and common excipient surfactants is dictated by the type of protein and its effective structuring/rigidity at the surface as reflected through surface elasticity. BSA was seen to exhibit a higher surface elasticity than lysozyme, and therefore has a more rigid structure and is more competitive at the interface. Poloxamer P188 does not exhibit high surface activity compared to proteins such as BSA or Lysozyme. Both PS 20 and PS 80 are able to displace BSA and Lysozyme at high concentrations. Rheological properties and thermal stability both seem to be impacted also by the choice of the surfactant. Thermal studies of BSA with each of the excipients show that the PS 20 results in the highest aggregation temperature. Additional studies are ongoing to understand the effects on thermal stability and rheology for lysozyme in the presence of these surfactants.

Investigating the Influence of Polysorbate 20/80 and Poloxamer P188 on the surface & interfacial properties of Bovine Serum Albumin and Lysozyme

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.