Protein-Surfactant and Protein-Protein Interactions During Freeze and Thaw: A Small-Angle Neutron Scattering Study of Lysozyme Solutions with Polysorbate and Poloxamer

Published

January 1, 2023

Author(s)

Xiaoda Yuan, Susan N. Krueger, Evgenyi Shalaev

Abstract

Protein structural changes during freezing and subsequent thawing are of great importance to a variety of biopharmaceutical applications. In this work, we studied the influence of non-ionic surfactants (polysorbate 20 and poloxamer 188) on protein structural changes during freeze and thaw using lysozyme as a model protein. Small-angle neutron scattering was employed to characterize protein structures in both liquid and frozen solution states. The results show minimal impact of polysorbate 20 on lysozyme structural changes during freeze and thaw using practically relevant concentrations. Poloxamer 188 seems to form interactions with lysozyme; when applied at high concentrations (10% w/w), such interaction prevents protein crowding or close packing typically resulted from freeze concentration. This study provides new insights into the unique properties of poloxamer 188 as a potential stabilizer for freezing applications.

Citation

Journal of Pharmaceutical Sciences

Volume

112

Pub Type

Journals

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DOI Link

Keywords

small-angle neutron scattering, polysorbate 20, poloxamer 188, freeze-thaw, protein stability, protein crowding

Citation

Yuan, X. , Krueger, S. and Shalaev, E. (2023), Protein-Surfactant and Protein-Protein Interactions During Freeze and Thaw: A Small-Angle Neutron Scattering Study of Lysozyme Solutions with Polysorbate and Poloxamer, Journal of Pharmaceutical Sciences, [online], https://dx.doi.org/10.1016/j.xphs.2022.08.017 (Accessed January 13, 2025)