科研之友
微信
新浪微博
Facebook
分享链接
摘要
Developing high-performance materials for efficient isolation of proteins is of great importance.Herein,the authors synthesized a series of magnetic Fe3O4@PS-ANTA-M~(2+)（M = Ni,Co,Cu and Zn)nanospheres,consisting of fine Fe3O4 nanoparticles encapsulated by functionalized polystyrene shell,where metal ions were complexed by Nα,Ncc-Bis（carboxymethyl)-L-lysine hydrate for selectively immobilizing histidine（His)-tagged proteins.The structures of the Fe3O4@PS-ANTA-M~(2+)were studied by field scanning electron microscopy,transmission microscopy,Fourier transform infrared spectroscopy,thermogravimetric analysis,X-ray photoelectron spectroscopy and vibrating sample magnetometer.The adsorption performance of the Fe3O4@PS-ANTA-M~(2+)was studied using bovine hemoglobin as a model protein.The thermodynamics of the binding process was studied by isothermal titration calorimetry tests.The resulting Fe3O4@PS-ANTA-Cu~(2+),Fe3O4@PS-ANTA-Ni~(2+),Fe3O4@PS-ANTA-Co~(2+)and Fe3O4@PS-ANTA-Zn~(2+)possessed adsorption capacities of 21200,8080,6640 and 5360 mg g~(-1)respectively,rendering them as the best adsorbents for protein purification.The adsorption isotherm was better fitted by Langmuir equation.To verify the selectivity,the Fe3O4@PS-ANTA-M~(2+)was practically employed to isolate His-tagged proteins from cell lysate.The results indicated that the samples showed outstanding adsorption capacity,selectivity and stability,and facile regeneration and separation,outperforming a commercial NTA-Ni column.These findings suggested that the Fe3O4@PS-ANTA-M~(2+)showed promising applications for specifically isolating proteins from complex biological systems.
- 单位
