Monitoring the thermally induced structural transitions of collagen by use of second-harmonic generation microscopy.
Monitoring the thermally induced structural transitions of collagen by use of second-harmonic generation microscopy.
复制标题
DOI：
10.1364/ol.30.000622
复制
发表时间：
2005-03
期刊：
影响因子：
3.6
通讯作者：
Sung-Jan Lin;Chih-Yuan Hsiao;Yen Sun;Wen Lo;Wei-Chou Lin;G. Jan;S. Jee;C. Dong
中科院分区：
文献类型：
--
作者：
Sung-Jan Lin;Chih-Yuan Hsiao;Yen Sun;Wen Lo;Wei-Chou Lin;G. Jan;S. Jee;C. Dong
用二次谐波显微镜研究了大鼠尾腱I型胶原的热裂解。我们研究了在25 ° C-60 ° C的温度范围内它对SHG图像和强度的影响。我们发现SHG信号在45 ℃开始迅速下降。然而，SHG成像显示，胶原纤维的断裂直到57 ℃才明显，并且随着温度的升高而增加。在57 ℃时，存在熔融和纤维状胶原蛋白的结构，并且胶原蛋白的破坏似乎在60 ℃时完成。我们的研究结果表明，除了强度测量，SHG成像是必要的监测细节的热诱导的胶原蛋白结构的变化在生物医学应用。
The thermal disruption of collagen I in rat tail tendon is investigated with second-harmonic generation (SHG) microscopy. We investigate its effects on SHG images and intensity in the temperature range 25 degrees-60 degrees C. We find that the SHG signal decreases rapidly starting at 45 degrees C. However, SHG imaging reveals that breakage of collagen fibers is not evident until 57 degrees C and worsens with increasing temperature. At 57 degrees C, structures of both molten and fibrous collagen exist, and the disruption of collagen appears to be complete at 60 degrees C. Our results suggest that, in addition to intensity measurement, SHG imaging is necessary for monitoring details of thermally induced changes in collagen structures in biomedical applications.