Ecosystem Sciences, Commonwealth Scientific and Industrial Research Organisation (CSIRO) , Clunies Ross Street, Acton, Australian Capital Territory 2601, Australia.
ACS Appl Mater Interfaces. 2014 Oct 22;6(20):18189-96. doi: 10.1021/am5051873. Epub 2014 Oct 1.
Viruses are important for a range of modern day applications. However, their utility is limited by their susceptibility to temperature degradation. In this study, we report a simple system to compare the ability of different dried protein films to stabilize viruses against exposure to elevated temperatures. Films from each of three different silks, silkworm, honeybee silk and hornet silk, stabilized entrapped viruses at 37 °C better than films of albumin from bovine serum (BSA) and all four proteins provided substantially more stabilization than no protein controls. A comparison of the molecular structure of the silks and BSA films showed no correlation between the ability of the proteins to stabilize the virus and the secondary structure of the protein in the films. The mechanism of stabilization is discussed and a hypothesis is suggested to explain the superior performance of the silk proteins.
病毒在现代的各种应用中非常重要。然而，由于它们对温度降解的敏感性，其用途受到限制。在这项研究中，我们报告了一种简单的系统，可以比较不同干燥蛋白质薄膜稳定病毒的能力，以抵抗高温暴露。来自三种不同丝的薄膜，蚕丝、蜜蜂丝和大黄蜂丝，比牛血清白蛋白（BSA）的薄膜更能稳定包埋的病毒在 37°C 下，并且所有四种蛋白质都比没有蛋白质对照提供了更多的稳定化。对丝和 BSA 薄膜的分子结构进行比较表明，蛋白质稳定病毒的能力与薄膜中蛋白质的二级结构之间没有相关性。讨论了稳定化的机制，并提出了一个假设来解释丝蛋白的优异性能。
