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首页> 外文期刊>Journal of Bioactive and Compatible Polymers >Microenvironmental changes in collagen/polyvinyl alcohol blends in the presence of ionic liquid: A spectroscopic analysis
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Microenvironmental changes in collagen/polyvinyl alcohol blends in the presence of ionic liquid: A spectroscopic analysis

机译:离子液体存在下胶原蛋白/聚乙烯醇混合物的微环境变化:光谱分析

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摘要

This study describes the microenvironmental changes due to various non-covalent interactions occurring in collagen/polyvinyl alcohol blends in the presence of ionic liquid, 1-butyl-3-methylimidazolium chloride, using spectroscopic techniques. These non-covalent interactions alter the hydration network of collagen. Electronic spectral analysis of collagen/polyvinyl alcohol/ionic liquid blends exhibited movement of tyrosine amino acid from the hydrophilic to hydrophobic core of collagen. Conformational studies investigating the influence of 1-butyl-3-methylimidazolium chloride on the intramolecular H-bonds revealed increased helicity packing and reorientation of H-bonds. This signifies that 1-butyl-3-methylimidazolium chloride is likely to be involved in reorienting the hydration dynamics of collagen, namely, by altering the existing and promoting formation of new intramolecular H-bonds between collagen and polyvinyl alcohol. Surface morphology of collagen/polyvinyl alcohol/ionic liquid blends revealed porous matrix, indicating 1-butyl-3-methylimidazolium chloride could act as a pore generator. This phenomenon can be employed for developing novel biomaterials with tunable porosity.
机译:这项研究使用光谱技术描述了在离子液体1-丁基-3-甲基咪唑鎓氯化物存在下,胶原蛋白/聚乙烯醇共混物中发生的各种非共价相互作用导致的微环境变化。这些非共价相互作用改变了胶原的水合网络。胶原/聚乙烯醇/离子液体混合物的电子光谱分析显示酪氨酸从胶原的亲水核到疏水核移动。构象研究调查了1-丁基-3-甲基咪唑鎓氯化物对分子内H键的影响,揭示了螺旋键的堆积和H键的重新定向增加。这表明1-丁基-3-甲基咪唑鎓氯化物可能参与重新定位胶原蛋白的水合动力学,即通过改变胶原蛋白和聚乙烯醇之间现有的分子内新的氢键并促进其形成。胶原蛋白/聚乙烯醇/离子液体共混物的表面形态揭示了多孔基质,表明氯化1-丁基-3-甲基咪唑鎓可作为造孔剂。这种现象可用于开发具有可调孔隙率的新型生物材料。

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