Thermal resilience of ensilicated lysozyme via calorimetric and in vivo analysis
Autor: | Lucy G. Weaver, Rémi Castaing, Aswin Doekhie, Asel Sartbaeva, L. Cliff, Joshua Paulin, Francoise Koumanov, J.M.H. van den Elsen, Yun-Chu Chen, Kevin J. Marchbank, Karen J. Edler, M. N. Slade |
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Rok vydání: | 2020 |
Předmět: |
0303 health sciences
General Chemical Engineering Thermal fluctuations In vivo analysis 02 engineering and technology General Chemistry 021001 nanoscience & nanotechnology Solvent 03 medical and health sciences chemistry.chemical_compound chemistry In vivo Thermal Biophysics Resilience (materials science) Lysozyme 0210 nano-technology Native structure 030304 developmental biology |
Zdroj: | RSC Advances. 10:29789-29796 |
ISSN: | 2046-2069 |
DOI: | 10.1039/d0ra06412b |
Popis: | Ensilication is a novel method of protein thermal stabilisation using silica. It uses a modified sol–gel process which tailor fits a protective silica shell around the solvent accessible protein surface. This, electrostatically attached, shell has been found to protect the protein against thermal influences and retains its native structure and function after release. Here, we report the calorimetric analysis of an ensilicated model protein, hen egg-white lysozyme (HEWL) under several ensilication conditions. DSC, TGA-DTA-MS, CD, were used to determine unfolding temperatures of native, released and ensilicated lysozyme to verify the thermal resilience of the ensilicated material. Our findings indicate that ensilication protects against thermal fluctuations even at low concentrations of silica used for ensilication. Secondly, the thermal stabilisation is comparable to lyophilisation, and in some cases is even greater than lyophilisation. Additionally, we performed a mouse in vivo study using lysozyme to demonstrate the antigenic retention over long-term storage. The results suggest that protein is confined within the ensilicated material, and thus is unable to unfold and denature but is still functional after long-term storage. |
Databáze: | OpenAIRE |
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