Thermal resilience of ensilicated lysozyme via calorimetric and in vivo analysis. Issue 50 (12th August 2020)
- Record Type:
- Journal Article
- Title:
- Thermal resilience of ensilicated lysozyme via calorimetric and in vivo analysis. Issue 50 (12th August 2020)
- Main Title:
- Thermal resilience of ensilicated lysozyme via calorimetric and in vivo analysis
- Authors:
- Doekhie, A.
Slade, M. N.
Cliff, L.
Weaver, L.
Castaing, R.
Paulin, J.
Chen, Y.-C.
Edler, K. J.
Koumanov, F.
Marchbank, K. J.
van den Elsen, J. M. H.
Sartbaeva, A. - Abstract:
- 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 protein to enable room temperature storage of biopharmaceuticals. 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-termAbstract : 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 protein to enable room temperature storage of biopharmaceuticals. 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. … (more)
- Is Part Of:
- RSC advances. Volume 10:Issue 50(2020)
- Journal:
- RSC advances
- Issue:
- Volume 10:Issue 50(2020)
- Issue Display:
- Volume 10, Issue 50 (2020)
- Year:
- 2020
- Volume:
- 10
- Issue:
- 50
- Issue Sort Value:
- 2020-0010-0050-0000
- Page Start:
- 29789
- Page End:
- 29796
- Publication Date:
- 2020-08-12
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d0ra06412b ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 13860.xml