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\begin{document}

\title{Polysorbate identity and quantity dictate the extensional flow
properties of protein-excipient solutions}



\author[1]{Kathleen Lauser}%
\author[1]{Amy Rueter}%
\author[1]{Michelle Calabrese}%
\affil[1]{University of Minnesota Twin Cities}%


\vspace{-1em}



  
  \date{May 19, 2024}


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\begin{abstract}
While protein medications are promising for treatment of cancer and
autoimmune diseases, challenges persist in terms of development and
injection stability of high-concentration formulations. Here, the
extensional flow properties of protein-excipient solutions are examined
via dripping-onto-substrate (DoS) extensional rheology, using a model
ovalbumin protein (OVA) and biocompatible excipients polysorbate 20
(PS20) and 80 (PS80). Despite similar PS structures, differences in
extensional flow are observed based on PS identity in two regimes: at
moderate total solution concentrations where surface tension differences
drive changes in extensional flow behavior, and at small PS:OVA ratios,
which impacts the onset of weakly elastic behavior. Undesirable
elasticity is observed in ultra-concentrated formulations, independent
of PS identity; higher PS contents are required to observe these effects
than with analogous polymeric excipient solutions. These studies reveal
novel extensional flow behaviors in protein-excipient solutions, and
provide a straightforward methodology for assessing the extensional flow
stability of new protein-excipient formulations.%
\end{abstract}%



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