Thermal stability, storage and release of proteins with tailored fit in silica.
Thermal stability, storage and release of proteins with tailored fit in silica.
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DOI：
10.1038/srep46568
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发表时间：
2017-04-24
影响因子：
4.6
通讯作者：
Sartbaeva A
中科院分区：
文献类型：
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作者：
Chen YC;Smith T;Hicks RH;Doekhie A;Koumanov F;Wells SA;Edler KJ;van den Elsen J;Holman GD;Marchbank KJ;Sartbaeva A
基于蛋白质的生物物质，包括疫苗、抗体和酶，通常在室温下随着时间的推移由于变性而降解，因为蛋白质随着二级和三级结构的损失而展开。因此，它们的储存和分配依赖于连续冷藏的“冷链”;这是昂贵的，而且并不总是有效的，因为冷链的任何中断都会导致效力和效力的迅速丧失。已经做出努力，使用包括冷冻干燥（冻干）、生物矿化和在糖玻璃和有机聚合物中封装的处理来使疫苗热稳定。在这里，我们第一次表明，蛋白质可以封闭在一个沉积的二氧化硅“笼”，使他们对变性热处理和长期的环境温度储存稳定，随后释放到溶液中，其结构和功能完好无损。这种“硅化”方法产生可储存的固体蛋白质负载材料，而不需要干燥或冷冻干燥。硅化为生物材料，特别是疫苗的“冷链”问题提供了解决方案的前景。
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.