Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center, Russian Academy of Sciences, Lobachevsky Str. 2/31, 420111 Kazan, Russia.
Laboratory of Chemistry and Technology of Marine Bioresources, Institute of Natural Science and Technology, Murmansk Arctic University, 183010 Murmansk, Russia.
Int J Mol Sci. 2024 Oct 31;25(21):11738. doi: 10.3390/ijms252111738.
We have studied the molecular properties of water in physically and chemically cross-linked gelatin hydrogels by FTIR-spectroscopy, NMR relaxation, and diffusivity and broadband dielectric spectroscopy, which are sensitive to dynamical properties of water, being a structural marker of polymer network. All experiments demonstrated definite reinforcement of the hydrogel net structure and an increase in the amount of hydrate water. FTIR experiments have shown that the chemical cross-linking of gelatin molecules initiates an increase in the collagen-like triple helices "strength", as a result of infused restriction on protein molecular mobility. The "strengthening" of protein chains hinders the mobility of protein fragments, introducing complex modifications into the structural properties of water which are remained practically unchanged up to up to 30-40 °C.
我们通过傅里叶变换红外光谱（FTIR）、NMR 弛豫、扩散和宽带介电光谱研究了物理和化学交联明胶水凝胶中的水分子的分子特性，这些技术对水的动力学性质敏感，是聚合物网络结构的标志。所有实验都表明水凝胶网络结构得到了明显增强，水合水量也有所增加。傅里叶变换红外光谱实验表明，明胶分子的化学交联会引发类似胶原蛋白的三螺旋“强度”增加，这是由于蛋白质分子流动性受到限制。蛋白质链的“加强”阻碍了蛋白质片段的流动性，从而对水的结构性质进行了复杂的修饰，这些修饰在 30-40°C 之间几乎保持不变。
