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Thermal resilience of ensilicated lysozyme via calorimetric and in vivo analysis

Lookup NU author(s): Professor Kevin Marchbank

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

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.


Publication metadata

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

Year: 2020

Volume: 10

Issue: 50

Pages: 29789-29796

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

URL: https://doi.org/10.1039/D0RA06412B

DOI: 10.1039/D0RA06412B


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