Journal
JOURNAL OF PHARMACEUTICAL SCIENCES
Volume 108, Issue 1, Pages 187-192Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.xphs.2018.06.016
Keywords
protein adsorption; polymer surface; bovine serum albumin (BSA); Hansen solubility parameters; cyclic olefin polymer; silicone; glass; contact angle; fluorescence microscopy
Funding
- West Pharmaceutical Service Inc.
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Hansen solubility parameters (HSP) theory has been successful in explaining the wettability of organic solvents on polymer surfaces and miscibility of different polymers. Here, we demonstrate that the amount of bovine serum albumin (BSA) protein adsorption on different polymer surfaces can also be explained by HSP. Interestingly, the HSP of the adsorbed BSA proteins calculated from the protein adsorption data is different than the HSP of native BSA protein itself. The HSP of the adsorbed BSA proteins are more hydrophobic than the native BSA protein. This observation suggested adsorbed BSA proteins are partially denatured and exposed their hydrophobic core toward the polymer surfaces. These results highlight a new strategic direction to understand interaction of protein with a surface: a theoretical approach that compliments experimental approach. The model in this study could be used to predict the amount of BSA adsorption on a polymer or any other solid surface, if the HSP of that surface is known. Further, the model can serve as a prescreen method to identify surfaces that are problematic at the outset and inform subsequent empirical studies to select packaging that will have the least adsorption for the specific biologic application. (C) 2019 American Pharmacists Association (R). Published by Elsevier Inc. All rights reserved.
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