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- W4385233428 abstract "Proteins make up vaccines, enzymes, and many types of therapeutics, so the stability of proteins is extremely important for the medical industry. Most protein-based pharmaceutical products require a temperature-controlled supply chain to ensure heat exposure does not disrupt the intermolecular interactions needed to maintain protein structure and product effectiveness. An innovative solution to the cold chain system has been developed using lactoferrin (Lf) as the model protein. In this study, the adsorption of lactoferrin (Lf) onto mesoporous silica significantly improved the thermal stability of this protein-based therapeutic. Lactoferrin adsorbed onto silica was heated above Lf’s denaturing temperature, and nonionic detergents were used to desorb Lf from the silica. Circular dichroism (CD) verified that the adsorbed Lf conserved a native secondary structure rich in α-helical content after the heat treatment. Lactoferrin desorption tests using nonionic detergents showed a trend for increased Lf recovery with increased detergent hydrophobicity. Triton X-100 and Tween 80 were the best detergents for Lf desorption, recovering over 80% of the initial protein. This case study provides strong evidence that Lf is thermally stabilized on mesoporous silica and efficiently released from the silica using nonionic detergents." @default.
- W4385233428 created "2023-07-26" @default.
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- W4385233428 date "2023-07-25" @default.
- W4385233428 modified "2023-09-23" @default.
- W4385233428 title "Thermal Stabilization of Lactoferrin via Sorption on Mesoporous Silica" @default.
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- W4385233428 doi "https://doi.org/10.1021/acs.jced.3c00021" @default.
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