摘要
采用傅里叶红外光谱和二维相关分析研究了改性前后胶原在升温(25～115℃)过程中结构的变化。结果显示,改性前后胶原的特征吸收峰强度降低,峰值向低波数移动,其中酰胺II带的变化最明显,降低了～10cm-1,表明维系胶原三股螺旋结构稳定的氢键被破坏,结构发生改变。在1 515cm-1处自相关峰强度最强,说明温度对酰胺II带的影响最大。与未改性胶原相比,改性胶原的相关程度更弱,表明改性胶原结构受温度影响要小,交联提高了胶原的热稳定性;改性后胶原结构变化的顺序也不一样。由此可见,二维红外相关分析法能提供由温度引起的胶原结构动态变化的微观信息,对进一步研究改性胶原结构和功能之间的关系有一定的意义。
The Fourier transform infrared spectroscopy and two dimensional correlation analysis method were applied to study a denaturing process of uncross-linked collagen and cross-linked collagen during varying temperature.It was found that the intensity of typically characteristic absorptions of collagen decreased and its peak shifted to low frequency,The amide II central absorbance peak moved to a lower frequency by about ～10 cm-1,which indicated that the inter-chain hydrogen bonds which stabilized the triple helix conformation of collagen were disrupted during thermal denaturation,resulting in a conformational change.The intensity of auto-peak at 1 515 cm-1 was maximum,which suggested that the temperature had a big impact on amide II.In comparison with uncross-linked collagen,the intensity of cross-peaks of cross-linked collagen was weaker,which demonstrated that the effect of temperature on the structure of cross-linked collagen was smaller,and the thermal stability properties of collagen solution could be improved by cross-linking.While the order of second structure changes of cross-linked collagen was different.These fundamental data should provide available information for understanding the relationship between the structure and function of cross-linked collagen.
出处
《光谱学与光谱分析》
SCIE
EI
CAS
CSCD
北大核心
2012年第6期1500-1506,共7页
Spectroscopy and Spectral Analysis
基金
国家自然科学基金项目(21076129)资助
关键词
交联胶原
二维红外相关光谱法
构象变化
Cross-linked collagen
Two-dimensional infrared correlation spectroscopy
Conformational change
