Structural properties of pepsin-solubilized collagen acylated by lauroyl chloride along with succinic anhydride.
Structural properties of pepsin-solubilized collagen acylated by lauroyl chloride along with succinic anhydride.
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DOI：
10.1016/j.msec.2015.05.055
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发表时间：
2015-10
期刊：
影响因子：
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通讯作者：
Conghu Li;Zhenhua Tian;Wentao Liu;Guoying Li
中科院分区：
文献类型：
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作者：
Conghu Li;Zhenhua Tian;Wentao Liu;Guoying Li
研究了月桂酰氯和琥珀酸酐酰化胃蛋白酶溶解小牛皮肤胶原蛋白的结构特性。氨基酸分析、圆二色性和x射线衍射结果表明，与天然胶原相比，酰化胶原保留了独特的三螺旋构象。同时，热重法测定的酰化胶原蛋白的热稳定性随着残余重量增加5%而增强。当温度从25℃升高到115℃时，利用傅里叶变换红外光谱测量，天然胶原和酰化胶原的二级结构被破坏，主要酰胺带的强度减小，主要酰胺带的位置向低波数偏移。同时，二维相关光谱显示，对酰化胶原和天然胶原最敏感的条带分别是酰胺I和酰胺II条带。此外，天然胶原与酰化胶原的基团对应顺序不同，且酰化胶原的相关程度弱于天然胶原，说明温度对酰化胶原构象的影响较小，可能是疏水相互作用提高了胶原的热稳定性。
The structural properties of pepsin-solubilized calf skin collagen acylated by lauroyl chloride along with succinic anhydride were investigated in this paper. Compared with native collagen, acylated collagen retained the unique triple helix conformation, as determined by amino acid analysis, circular dichroism and X-ray diffraction. Meanwhile, the thermostability of acylated collagen using thermogravimetric measurements was enhanced as the residual weight increased by 5%. With the temperature increased from 25 to 115 °C, the secondary structure of native and acylated collagens using Fourier transform infrared spectroscopy measurements was destroyed since the intensity of the major amide bands decreased and the positions of the major amide bands shifted to lower wavenumber, respectively. Meanwhile, two-dimensional correlation spectroscopy revealed that the most sensitive bands for acylated and native collagens were amide I and II bands, respectively. Additionally, the corresponding order of the groups between native and acylated collagens was different and the correlation degree for acylated collagen was weaker than that of native collagen, suggesting that temperature played a small influence on the conformation of acylated collagen, which might be concluded that the hydrophobic interaction improved the thermostability of collagen.