4.7 Article

Thermal stability, storage and release of proteins with tailored fit in silica

期刊

SCIENTIFIC REPORTS
卷 7, 期 -, 页码 -

出版社

NATURE PUBLISHING GROUP
DOI: 10.1038/srep46568

关键词

-

资金

  1. University of Bath
  2. EPSRC Centre for Doctoral Training in Sustainable Chemical Technologies [EP/L016354/1]
  3. Annett Trust
  4. Royal Society
  5. Alumni Fund
  6. MRC [MR/J003417/1]
  7. European Research Council (ERC) under the European Union's Horizon research and innovation programme [648283]
  8. ESRF
  9. European Research Council (ERC) [648283] Funding Source: European Research Council (ERC)
  10. Medical Research Council [MR/P002927/1, MC_PC_15030] Funding Source: researchfish
  11. MRC [MR/J003417/1, MC_PC_15030, MR/P002927/1] Funding Source: UKRI

向作者/读者索取更多资源

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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据