Synthesis of magnetic Fe3O4@PS-ANTA-M2+ (M = Ni, Co, Cu and Zn) nanospheres for specific isolation of histidine-tagged proteins

[Display omitted] •Core-shelled Fe3O4@PS-ANTA-M2+ (M = Ni, Co, Cu and Zn) nanospheres were synthesized.•The samples showed outstanding capacities and selectivities for isolating his-tagged proteins.•The resulting Fe3O4@PS-ANTA-Cu2+ possessed a maximum adsorption capacity of 21.2 g g−1.•The samples a...

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Veröffentlicht in:Chemical engineering journal (Lausanne, Switzerland : 1996) Switzerland : 1996), 2021-01, Vol.404, p.126427, Article 126427
Hauptverfasser: Ge, Moyan, Zhang, Jiali, Gai, Zuoqi, Fan, Renshui, Hu, Songqing, Liu, Guo, Cao, Yong, Du, Xilong, Shen, Yi
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Sprache:eng
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Zusammenfassung:[Display omitted] •Core-shelled Fe3O4@PS-ANTA-M2+ (M = Ni, Co, Cu and Zn) nanospheres were synthesized.•The samples showed outstanding capacities and selectivities for isolating his-tagged proteins.•The resulting Fe3O4@PS-ANTA-Cu2+ possessed a maximum adsorption capacity of 21.2 g g−1.•The samples also exhibited facile magnetic separation and excellent stability. Developing high-performance materials for efficient isolation of proteins is of great importance. Herein, the authors synthesized a series of magnetic Fe3O4@PS-ANTA-M2+ (M = Ni, Co, Cu and Zn) nanospheres, consisting of fine Fe3O4 nanoparticles encapsulated by functionalized polystyrene shell, where metal ions were complexed by Nα, Nα-Bis(carboxymethyl)-L-lysine hydrate for selectively immobilizing histidine (His)-tagged proteins. The structures of the Fe3O4@PS-ANTA-M2+ 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-M2+ 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-Cu2+, Fe3O4@PS-ANTA-Ni2+, Fe3O4@PS-ANTA-Co2+ and Fe3O4@PS-ANTA-Zn2+ 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-M2+ 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-M2+ showed promising applications for specifically isolating proteins from complex biological systems.
ISSN:1385-8947
1873-3212
DOI:10.1016/j.cej.2020.126427