Department of Biological and Biochemical Sciences, Faculty of Chemical Technology, University of Pardubice , Studentska 573, 532 10 Pardubice, Czech Republic.
Center of Materials and Nanotechnologies, Faculty of Chemical Technology, University of Pardubice , Nam. Cs. Legii 565, 530 02 Pardubice, Czech Republic.
ACS Appl Mater Interfaces. 2017 Aug 30;9(34):28233-28242. doi: 10.1021/acsami.7b08445. Epub 2017 Aug 21.
In this work, a high surface area interface, based on anodic one-dimensional (1D) TiO nanotubes homogeneously decorated by FeO nanoparticles (TiONTs@FeONPs) is reported for the first time for an unprecedented purification of His-tagged recombinant proteins. Excellent purification results were achieved from the model protein mixture, as well as from the whole cell lysate (with His-tagged ubiquitin). Compared to a conventional immobilized-metal affinity chromatography (IMAC) system, specific isolation of selected His-tagged proteins on behalf of other proteins was significantly enhanced on TiONTs@FeONPs interface under optimized binding and elution conditions. The combination of specific isolation properties, magnetic features, biocompatibility, and ease of preparation of this material consisting of two basic metal oxides makes it a suitable candidate for future purification of recombinant proteins in biotechnology. The principally new material bears a large potential to open new pathways for discoveries in nanobiotechnology and nanomedicine.
在这项工作中，首次报道了基于阳极一维（1D）TiO 纳米管均匀修饰的 FeO 纳米颗粒（TiONTs@FeONPs）的高表面积界面，用于空前地纯化 His 标记的重组蛋白。从模型蛋白混合物以及含 His 标记泛素的全细胞裂解物中都获得了优异的纯化结果。与传统的固定化金属亲和层析（IMAC）系统相比，在优化的结合和洗脱条件下，TiONTs@FeONPs 界面上显著增强了对所选 His 标记蛋白相对于其他蛋白的特异性分离。这种由两种基本金属氧化物组成的材料具有特异性分离特性、磁性、生物相容性和易于制备的特点，使其成为未来生物技术中重组蛋白纯化的合适候选材料。这种新型材料具有很大的潜力，可以为纳米生物技术和纳米医学的发现开辟新途径。
