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Lookup NU author(s): Professor Kevin MarchbankORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
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.
Author(s): Doekhie A, Slade MN, Cliff L, Weaver L, Castaing R, Paulin J, Chen Y-C, Edler KJ, Koumanov F, Marchbank KJ, van den Elsen JMH, Sartbaeva A
Publication type: Article
Publication status: Published
Journal: RCS Advances
Online publication date: 12/08/2020
Acceptance date: 04/08/2020
Date deposited: 05/08/2020
ISSN (electronic): 2046-2069
Publisher: Royal Society of Chemistry
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