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首页> 外文期刊>Journal of Inclusion Phenomena and Macrocyclic Chemistry >Protein stabilization through supramolecular host–guest interactions with cyclodextrin-modified nanoparticles
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Protein stabilization through supramolecular host–guest interactions with cyclodextrin-modified nanoparticles

机译:通过超分子宿主-客体与环糊精修饰的纳米粒子相互作用来稳定蛋白质

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摘要

This study demonstrates the protein stabilization of gelatin through supramolecular interactions of silica nanoparticles and the influence on the point of denaturation. The phenomenon was studied in diluted solutions by dynamic light scattering, viscosity measurements, and differential scanning calorimetry. Native gelatin is stabilized by cyclodextrin functionalized SiO2 nanoparticles. After heating, increased supramolecular interactions of the nanoparticles with the denaturated gelatin coils are observed by progressive agglomeration. The described observation also resulted in a melting temperature shift from 30 °C, for native gelatin, to about 47 °C for the gelatin/CD-SiO2, which indicates the supramolecular stabilization of the gelatin chain structure. It was found that the gelatin is supramolecularly immobilized on the nanoparticle up to a certain temperature through complexation by cyclodextrin. The described results, also confirmed by DSC and viscosity measurements, show the prospect of using cyclodextrin-modified surfaces for the immobilization of the proteins.
机译:这项研究表明通过二氧化硅纳米粒子的超分子相互作用以及对变性点的影响,明胶的蛋白质稳定作用。在稀释溶液中通过动态光散射,粘度测量和差示扫描量热法研究了该现象。天然明胶被环糊精官能化的SiO 2 纳米颗粒稳定。加热后,通过逐步团聚观察到纳米粒子与变性明胶线圈的超分子相互作用增加。所描述的观察结果还导致天然明胶的熔化温度从30°C转变为明胶/ CD-SiO 2 的约47°C,这表明明胶链结构的超分子稳定性。已经发现明胶通过环糊精的络合而超分子地固定在纳米颗粒上直至一定温度。所述结果也通过DSC和粘度测量证实,显示出使用环糊精修饰的表面固定蛋白质的前景。

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