胶原分子酰化修饰对其结构与性能的影响

发布时间：2018-06-12 17:56

本文选题：胶原 + 酰化　；参考：《高分子材料科学与工程》2016年01期

【摘要】：在碱性条件下,采用琥珀酸酐(SA)、马来酸酐(MA)、邻苯二甲酸酐(PA)对提取的酶溶性胶原进行分子修饰,并通过总碳含量、等电点、红外、X射线衍射、圆二色谱、超灵敏差示扫描量热以及体外成纤等方法对酰化前后胶原的结构与性能进行了表征。结果表明,酸酐改性后的胶原侧链羧基含量明显增加,等电点显著下降,且酰化后的胶原仍保有特殊的三股螺旋构象;不同修饰程度的琥珀酰化胶原的红外、圆二色谱表明,胶原的酰化程度越高,其三股螺旋构象的完整性越差。与PA改性胶原相比,SA、MA酰化胶原有着更完整的三股螺旋构象和更高的热变性温度。体外成纤实验显示,酰化胶原不具备生理条件下的成纤能力,表明三股螺旋结构是胶原成纤的必要不充分条件。
[Abstract]:The enzyme soluble collagen was modified with succinic anhydride, maleic anhydride and phthalic anhydride PAA under alkaline conditions, and was modified by total carbon content, isoelectric point, infrared X-ray diffraction, circular dichroism. The structure and properties of collagen before and after acylation were characterized by hypersensitive differential scanning calorimetry and fiber formation in vitro. The results showed that the carboxyl content of collagen modified by acetic anhydride was obviously increased, the isoelectric point was significantly decreased, and the acylated collagen still retained special three-strand helix conformation. The infrared spectra and circular dichroism of succinylated collagen with different degree of modification showed that the content of carboxyl group in collagen modified by acetic anhydride was obviously increased, and the isoelectric point was decreased significantly. The higher the acylation degree of collagen, the worse the integrity of three helix conformation. Compared with PA modified collagen, the acylated collagen has a more complete triple helix conformation and higher thermal denaturation temperature. In vitro fibrillation experiments showed that acylated collagen did not possess the ability to form fibers under physiological conditions, which indicated that the three-stranded helical structure was the necessary and insufficient condition for the formation of collagen fibers.
【作者单位】：四川大学皮革化学与工程教育部重点实验室;齐鲁工业大学皮革化学与工程学院;
【基金】：国家自然科学基金资助项目(51273128;20976110)
【分类号】：O629.73

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