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首页> 外文期刊>RSC Advances >Insights into the interactions between porcine collagen and a Zr-Al-Ti metal complex
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Insights into the interactions between porcine collagen and a Zr-Al-Ti metal complex

机译：深入了解猪胶原蛋白与Zr-Al-Ti金属络合物之间的相互作用

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摘要

Porcine acelluar dermal matrix (pADM), known as pure collagen with three dimensional structure, was used to explore the interactions between porcine collagen and a metal complex in this study. The metal complex mainly consists of elements Zr, Al and Ti (patented product named DMT-II). Tests of Fourier transform infrared spectrometry (FTIR), the crosslinking degree, Diffraction Scanning Calorimetry (DSC), Scanning Electron Microscopy (SEM) and X-ray diffraction (XRD) were carried out to further probe the microscopic changes between collagen and the metal complex. Results have revealed that the DMT-II could react with collagen between fibers and at functional groups in the collagen molecules. The unique structure of collagen has been retained with only small changes of intensity of the characteristic absorption peaks appeared. The highest thermal denaturation temperature of pADM after reaction with DMT-II (50%) was 86.6 degrees C, which has been improved by 18.9 degrees C. The crystal structure analyzed by XRD showed that DMT-II affected the triple helical structure of collagen to some degree, proving that the reaction took place at the collagen molecules. Through morphology observation, it was clear that DMT-II changed the fiber distribution, and the fibers in pADM assembled together to form a tight layer. By a series of tests, results showed that the reaction between collagen and DMT-II could take place both in fibers and in collagen molecules, which paved a new way for collagen modification.
机译：猪细胞真皮基质（pADM），被称为具有三维结构的纯胶原蛋白，用于研究猪胶原蛋白和金属络合物之间的相互作用。金属络合物主要由元素Zr，Al和Ti组成（专利产品为DMT-II）。进行了傅里叶变换红外光谱（FTIR），交联度，衍射扫描量热法（DSC），扫描电子显微镜（SEM）和X射线衍射（XRD）的测试，以进一步探查胶原蛋白与金属配合物之间的微观变化。 。结果表明，DMT-II可以与纤维之间以及胶原分子中的官能团反应。胶原蛋白的独特结构得以保留，仅出现特征吸收峰强度的微小变化。与DMT-II（50％）反应后，pADM的最高热变性温度为86.6℃，提高了18.9℃。XRD分析的晶体结构表明DMT-II影响胶原的三螺旋结构。在某种程度上证明了该反应发生在胶原分子上。通过形态观察，很明显DMT-II改变了纤维分布，pADM中的纤维组装在一起形成紧密层。通过一系列测试，结果表明胶原蛋白与DMT-II之间的反应既可以在纤维中也可以在胶原蛋白分子中发生，这为胶原蛋白修饰开辟了一条新途径。

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