Raman spectroscopic study of glutaraldehyde-stabilized collagen and pericardium tissue
Raman spectroscopic study of glutaraldehyde-stabilized collagen and pericardium tissue
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DOI：
10.1163/156856203321142605
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发表时间：
2003-01-01
影响因子：
3.6
通讯作者：
Cwalina, B
中科院分区：
文献类型：
--
作者：
Jastrzebska, M;Wrzalik, R;Cwalina, B
拉曼光谱首次用于研究戊二醛 (GA) 处理后胶原蛋白和猪心包组织中交联的形成。 GA 处理会产生非常高的荧光背景，与拉曼谱带重叠。研究发现，较短的固定时间（即2小时）可显着降低背景辐射，为研究GA修饰后胶原蛋白分子结构的变化提供了新的可能性。观察到的拉曼带位置和强度的变化使我们能够识别不同类型的 GA-胶原蛋白相互作用。已发现强有力的光谱证据证明肽对 GA 胶原交联的形成以及通过席夫碱中间体和吡啶鎓型交联形成仲胺的贡献。结果还表明，与胶原蛋白制剂相比，不同的水合水平和完整组织更复杂的结构强烈影响 GA 交联网络的形成，例如优选在水合程度较低的胶原制剂中形成醚型键。我们的结果表明，GA 治疗会导致心包组织和胶原蛋白的含水量增加。
For the first time, Raman spectroscopy has been employed to investigate formation of cross-links in collagen and porcine pericardium tissue upon glutaraldehyde (GA) treatment. GA treatment causes a very high fluorescence background, which overlaps Raman bands. It has been found that short fixation time, i.e. 2 h, reduces background radiation significantly, providing new possibilities for studying changes in molecular structure of collagen upon GA modification. The observed changes in position and intensity of Raman bands allowed us to recognize different types of GA-collagen interactions. Strong spectral evidence has been found for the peptide contribution to the formation of the GA-collagen cross-links and for the formation of secondary amines via Schiff base intermediates, and pyridinium-type cross-links. The results also revealed that different hydration levels and a more complex structure of intact tissue in comparison to collagen preparation strongly influence the formation of a GA cross-linking network, e.g. ether-type bond is preferred to form in a less hydrated collagen preparation. Our results have shown that GA treatment causes an increase in water content of pericardium tissue and collagen.