Thermal stability, storage and release of proteins with tailored fit in silica
(2017) In Scientific Reports 7.- Abstract
Biological substances based on proteins, including vaccines, antibodies, and enzymes, typically degrade at room temperature over time due to denaturation, as proteins unfold with loss of secondary and tertiary structure. Their storage and distribution therefore relies on a “cold chain” of continuous refrigeration; this is costly and not always effective, as any break in the chain leads to rapid loss of effectiveness and potency. Efforts have been made to make vaccines thermally stable using treatments including freeze-drying (lyophilisation), biomineralisation, and encapsulation in sugar glass and organic polymers. Here for the first time we show that proteins can be enclosed in a deposited silica “cage”, rendering them stable against... (More)
Biological substances based on proteins, including vaccines, antibodies, and enzymes, typically degrade at room temperature over time due to denaturation, as proteins unfold with loss of secondary and tertiary structure. Their storage and distribution therefore relies on a “cold chain” of continuous refrigeration; this is costly and not always effective, as any break in the chain leads to rapid loss of effectiveness and potency. Efforts have been made to make vaccines thermally stable using treatments including freeze-drying (lyophilisation), biomineralisation, and encapsulation in sugar glass and organic polymers. Here for the first time we show that proteins can be enclosed in a deposited silica “cage”, rendering them stable against denaturing thermal treatment and long-term ambient-temperature storage, and subsequently released into solution with their structure and function intact. This “ensilication” method produces a storable solid protein-loaded material without the need for desiccation or freeze-drying. Ensilication offers the prospect of a solution to the “cold chain” problem for biological materials, in particular for vaccines.
(Less)
- author
- publishing date
- 2017
- type
- Contribution to journal
- publication status
- published
- in
- Scientific Reports
- volume
- 7
- article number
- 46568
- publisher
- Nature Publishing Group
- external identifiers
-
- pmid:28436442
- scopus:85038898791
- ISSN
- 2045-2322
- DOI
- 10.1038/srep46568
- language
- English
- LU publication?
- no
- additional info
- Publisher Copyright: © The Author(s) 2017
- id
- ae963ac0-fb61-45d6-9387-5566628ce8e3
- date added to LUP
- 2023-01-18 09:14:04
- date last changed
- 2024-07-26 20:13:58
@article{ae963ac0-fb61-45d6-9387-5566628ce8e3, abstract = {{<p>Biological substances based on proteins, including vaccines, antibodies, and enzymes, typically degrade at room temperature over time due to denaturation, as proteins unfold with loss of secondary and tertiary structure. Their storage and distribution therefore relies on a “cold chain” of continuous refrigeration; this is costly and not always effective, as any break in the chain leads to rapid loss of effectiveness and potency. Efforts have been made to make vaccines thermally stable using treatments including freeze-drying (lyophilisation), biomineralisation, and encapsulation in sugar glass and organic polymers. Here for the first time we show that proteins can be enclosed in a deposited silica “cage”, rendering them stable against denaturing thermal treatment and long-term ambient-temperature storage, and subsequently released into solution with their structure and function intact. This “ensilication” method produces a storable solid protein-loaded material without the need for desiccation or freeze-drying. Ensilication offers the prospect of a solution to the “cold chain” problem for biological materials, in particular for vaccines.</p>}}, author = {{Chen, Yun-Chu and Smith, Tristan and Hicks, Robert H. and Doekhie, Aswin and Koumanov, Francoise and Wells, Stephen A. and Edler, Karen J. and van den Elsen, Jean and Holman, Geoffrey D. and Marchbank, Kevin J. and Sartbaeva, Asel}}, issn = {{2045-2322}}, language = {{eng}}, publisher = {{Nature Publishing Group}}, series = {{Scientific Reports}}, title = {{Thermal stability, storage and release of proteins with tailored fit in silica}}, url = {{http://dx.doi.org/10.1038/srep46568}}, doi = {{10.1038/srep46568}}, volume = {{7}}, year = {{2017}}, }