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 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.

Original languageEnglish
Article number46568
Pages (from-to)1-8
Number of pages8
JournalScientific Reports
Volume7
Early online date24 Apr 2017
DOIs
Publication statusPublished - 24 Apr 2017

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Refrigeration
Freeze Drying
Silicon Dioxide
Vaccines
Hot Temperature
Desiccation
Protein Unfolding
Proteins
Temperature
Glass
Polymers
Antibodies
Enzymes
Therapeutics

Keywords

  • Journal Article

Cite this

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title = "Thermal stability, storage and release of proteins with tailored fit in silica",
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 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.",
keywords = "Journal Article",
author = "Yun-Chu Chen and Tristan Smith and Hicks, {Robert H} and Aswin Doekhie and Francoise Koumanov and Wells, {Stephen A} and Edler, {Karen J} and {van den Elsen}, Jean and Holman, {Geoffrey D} and Marchbank, {Kevin J} and Asel Sartbaeva",
year = "2017",
month = "4",
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T1 - Thermal stability, storage and release of proteins with tailored fit in silica

AU - Chen, Yun-Chu

AU - Smith, Tristan

AU - Hicks, Robert H

AU - Doekhie, Aswin

AU - Koumanov, Francoise

AU - Wells, Stephen A

AU - Edler, Karen J

AU - van den Elsen, Jean

AU - Holman, Geoffrey D

AU - Marchbank, Kevin J

AU - Sartbaeva, Asel

PY - 2017/4/24

Y1 - 2017/4/24

N2 - 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.

AB - 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.

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