Gąsior-Głogowska Marlena, Komorowska Małgorzata, Hanuza Jerzy, Ptak Maciej, Kobielarz Magdalena
Institute of Biomedical Engineering and Instrumentation, Wrocław University of Technology, Wrocław, Poland.
Acta Bioeng Biomech. 2010;12(4):55-62.
Fourier Transform Near Infrared Raman Spectroscopy has been used to monitor the molecular changes of collagen in a tendon subjected to strain. In the Raman spectrum of the unstrained tendon, some protein bands, mainly assigned to collagen, can be observed: amide I (1666 cm-1) and III (1266 and 1248 cm-1) vibrational modes and skeletal (C-C) stretching vibrations (816 and 940 cm-1). The position of these bands is changing with the increasing strain values. It is concluded that elastin and non-helical domains of collagen are initially involved in the load transfer and triple helices of collagen are gradually joining this process.
傅里叶变换近红外拉曼光谱已被用于监测受应变作用的肌腱中胶原蛋白的分子变化。在未受应变的肌腱的拉曼光谱中，可以观察到一些主要归属于胶原蛋白的蛋白质谱带：酰胺I（1666厘米-1）和III（1266和1248厘米-1）振动模式以及骨架（C-C）伸缩振动（816和940厘米-1）。这些谱带的位置随着应变值的增加而变化。得出的结论是，弹性蛋白和胶原蛋白的非螺旋结构域最初参与了载荷传递，而胶原蛋白的三螺旋结构逐渐加入这一过程。
