Investigating Buffer Effects on Lysozyme Adsorption to Borosilicate Glass

Abstract

Protein adsorption refers to the accumulation and adherence of a protein to the surface of a solid, but without surface, penetration occurring. Proteins can adsorb to a variety of interfaces that are used in the manufacture, formulation, and storage of protein medicines. This can have unintended consequences such as a loss of expensive protein products and aggregate formation. This study investigates the role of buffer composition, pH, and protein concentration on the adsorption of lysozyme to borosilicate glass. Using reverse-phase HPLC and differential scanning fluorimetry, we quantified the mass of adsorbed lysozyme and assessed the stability of lysozyme in each buffer system. The highest amount of adsorbed lysozyme occurred in the sodium phosphate and histidine-HCl buffers at pH 7.4 and stability analysis showed that lysozyme had the lowest melt temperature in these buffers.

Keywords

Protein Adsorption, Buffer, Stability, Borosilicate

How to Cite

Downey, J. D., Crean, A. & Ryan, K. B., (2022) “Investigating Buffer Effects on Lysozyme Adsorption to Borosilicate Glass”, British Journal of Pharmacy 7(2). doi: https://doi.org/10.5920/bjpharm.1157

Funding

  • European Regional Development Fund and EPSRC-CDT and the Engineering and Physical Sciences Research Council UK
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Authors

John Donal Downey (University College Cork)
Abina Crean (University College Cork)
Katie B Ryan (University College Cork)

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Creative Commons Attribution 4.0

Competing Interests

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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This article has been peer reviewed.

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