Non-invasive characterization of the elastic protein resilin in insects using Raman spectroscopy
Non-invasive characterization of the elastic protein resilin in insects using Raman spectroscopy
复制标题
使用拉曼光谱法非侵入性地表征昆虫中弹性蛋白的弹性蛋白
DOI：
10.1016/j.ijbiomac.2023.127967
复制
发表时间：
2024
影响因子：
8.2
通讯作者：
Gonzalez-Rodriguez, Jose
中科院分区：
文献类型：
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作者：
Woodrow, Charlie;Cullen, Darron A.;Montealegre-Z, Fernando;Gonzalez-Rodriguez, Jose
节肢弹性蛋白是一种在昆虫运动部位发现的极其有效的弹性蛋白。尽管对节肢动物进行了多年的研究，我们仍然刚刚开始了解它的多样性、天然结构和功能。了解节肢弹性蛋白结构和多样性的差异可能会导致仿生弹性聚合物的开发，在材料科学中具有广泛的应用。在这里，为了更好地了解节肢动物的结构，我们提供了一种新的方法，使用非侵入性拉曼光谱在模型物种沙漠蝗虫（Schistocerca gregaria）中识别昆虫角质层富含节肢动物的区域。将后腿富含弹性蛋白的半月突的拉曼光谱与附近低弹性蛋白角质层的拉曼光谱进行比较，并为这两个区域分配参考光谱和峰值。节肢素的主峰包括在 955–962 和 1141–1203 cm−1 处与酪氨酸相关的两个谱带，以及在 1615 cm−1 处的一个强峰，归因于与二酪氨酸相关的 α-酰胺 I 基团。我们还发现 ~485–567 cm−1 的几丁质骨骼模式对各组之间的光谱差异有重要贡献。作为对照技术，拉曼光谱也与荧光光谱获得的结果进行了比较。对这些所得光谱的主成分分析揭示了富含节肢弹性蛋白和缺乏节肢弹性蛋白的角质层区域的光散射特性的差异，这可能与天然蛋白质结构和相对丰度的差异有关。
Resilin is an extremely efficient elastic protein found in the moving parts of insects. Despite many years of resilin research, we are still only just starting to understand its diversity, native structures, and functions. Understanding differences in resilin structure and diversity could lead to the development of bioinspired elastic polymers, with broad applications in materials science. Here, to better understand resilin structure, we offer a novel methodology for identifying resilin-rich regions of the insect cuticle using non-invasive Raman spectroscopy in a model species, the desert locust (Schistocerca gregaria). The Raman spectrum of the resilin-rich semilunar process of the hind leg was compared with that of nearby low-resilin cuticle, and reference spectra and peaks assigned for these two regions. The main peaks of resilin include two bands associated with tyrosine at 955–962 and 1141–1203 cm−1and a strong peak at 1615 cm−1, attributed to the α-Amide I group associated with dityrosine. We also found the chitin skeletal modes at ~485–567 cm−1to be significant contributors to spectra variance between the groups. Raman spectra were also compared to results obtained by fluorescence spectroscopy, as a control technique. Principal component analysis of these resulting spectra revealed differences in the light-scattering properties of resilin-rich and resilin-poor cuticular regions, which may relate to differences in native protein structure and relative abundance.