关节软骨内胶原纤维各向异性的红外光谱学显微成像研究

福尔马林溶液对于固化关节软骨组织、防止在长时间测量过程中组织的分解退化起到很好的作用，但对福尔马林溶液浸泡后软骨组织的结构变化(固化)过程及其胶原纤维各向异性的改变却鲜有研究。采用傅里叶变换红外光谱显微成像技术与偏振技术相结合的方法，通过关节软骨内胶原纤维(蛋白)的红外光谱特征吸收峰(Amide Ⅰ，Amide Ⅱ带)的吸光度随福尔马林溶液浸泡时间及偏光角度的变化来研究福尔马林溶液对软骨组织结构即胶原纤维各向异性的影响，并利用与各向异性方程拟合得到的决定系数(R2)对胶原蛋白纤维各向异性程度进行表征。研究发现，关节软骨Amide Ⅰ和Amide Ⅱ带的各向异性随着福尔马林浸泡时间的增长而愈加明显(Amide Ⅰ带变化尤为明显)，说明福尔马林溶液中甲醛分子诱发了胶原蛋白分子新的交联，最终获得较好的固化效果，有利于关节软骨的各向异性分析。本研究将为今后关节软骨样本的制备、储存及各向异性研究提供参考。

Study on the Anisotropy of Collagenours Fibers in Articular with Infrared Imagi ng

Formalin solution has been widely used to solidify the organization of articular cartilage and prevent tissue decomposi‐tion in long‐time measurement .However ,it was rarely investigated that the structural anisotropy changes of collagen fiber (fixa‐tion) of articular cartilage when it was immersed in formalin .In this paper ,Fourier transform infrared spectroscopic imaging with polarization technique was used to investigate the anisotropic structure change of collagen fiber of articular cartilage fixed in formalin through the absorbance change of Amide I and Amide II with immersing time and polarization direction .The degree of anisotropy of collagen fiber in cartilage was characterized with fitting related coefficient of absorbance .The anisotropy of Amide I and Amide II became stronger with immersing extension of articular cartilage in formalin ,and the amide I showed more remark‐able anisotropy .It was concluded that the formalin solution induced new crosslinks of collagen ,which gradually strengthened the collagen fiber anisotropy and was helpful for the structural analysis of the articular cartilage .The study will be significant for the preparation ,preservation and anisotropy research of cartilage specimen .