Effect of Low-Temperature Plasma Jet on Thermal Stability and Physical Structure of Type I Collagen
Effect of Low-Temperature Plasma Jet on Thermal Stability and Physical Structure of Type I Collagen
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DOI：
10.1109/tps.2012.2190303
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发表时间：
2012-06-01
影响因子：
1.5
通讯作者：
Lacabanne, Colette
中科院分区：
文献类型：
--
作者：
Samouillan, Valerie;Merbahi, Nofel;Lacabanne, Colette
这项工作是专门的I型胶原蛋白处理的低温等离子体射流在环境空气中产生的，以确定是否得到的纤维材料的结构保存或加强的表征。通过差示扫描量热法（DSC）检查胶原蛋白的物理结构，差示扫描量热法是分析蛋白质中的热转变（例如变性）的非常合适的技术。DSC用于评价等离子体处理后胶原蛋白的热稳定性，而傅立叶变换红外光谱用于检查三螺旋结构域的完整性，并研究等离子体处理对胶原蛋白官能团的影响。更具体地显示，等离子体处理可以稳定胶原结构而不改变三螺旋结构。这一观察结果得到以下结果的支持：1）观察到胶原变性向高温范围的转变，2）与对照样品相比，交联作用使链变硬。
This work is devoted to the characterization of type I collagen treated by a low-temperature plasma jet generated in ambient air to determine whether the resulting fibrous material is structurally preserved or reinforced. The physical structure of collagen is checked by differential scanning calorimetry (DSC), which is a well suited technique to analyze thermal transitions in proteins, such as denaturation. DSC is used to evaluate the thermal stability of collagen after the plasma treatments while Fourier transform infra red spectroscopy is used to check the integrity of triple helical domain and to investigate the effects of plasma treatments on the functional groups of collagen. It is more particularly shown that the plasma treatment can stabilize the collagen structure without altering the triple helical structure. This observation is supported by 1) the shift observed toward high-temperature range of the collagen denaturation and 2) the stiffening of the chains by a cross-linking action when compared to the control sample.