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Citation: LI Qiang, JI Xiao-Xu, ZHONG Qiu, HUANG Xin-Tang, XIONG Li. Ultrafine ZnFe2O4 Nanocrystals Interacting with Proteins[J]. Chinese Journal of Inorganic Chemistry, ;2013, 29(11): 2375-2381. doi: 10.3969/j.issn.1001-4861.2013.00.368 shu

Ultrafine ZnFe2O4 Nanocrystals Interacting with Proteins

  • 1.

    1 Institute of Nanoscience and Nanotechnology, Central China Normal University, Wuhan 430079, China;

  • Received Date: 8 May 2013
    Available Online: 20 June 2013

    Fund Project: 国家自然科学基金(No.51172085)资助项目。 (No.51172085)

  • Ultrafine ZnFe2O4 nanocrystals were prepared by hydrothermal method and characterized by HRTEM, XRD and EDX techniques respectively. Protein adsorption properties and their correlations to ζ potentials between nanocrystals and protein molecules were investigated under different pH conditions using bovine serum albumin (BSA) and hemoglobin as model proteins. The hydrodynamic size of bare and protein loaded nanocrystals as well as protein conformation changes induced by nanocrystals were respectively studied by dynamic light scattering (DLS) and Fourier transform infrared (FTIR) spectroscopy techniques. Results show that adsorption between nanocrystals and hemoglobin obeys the law of electrostatistic interaction, whereas BSA adsorption behavior is not agreed with such law. After hemoglobin loading, most of nanocrystal-protein systems suspend as monomers and trimers apart from a few aggregates, whereas only aggregates exist after BSA adsorbing onto nanocrystals. FTIR spectroscopy revealed that Hemoglobin suffers more conformational changes than that of BSA. In addition, highly protein adsorption capacities exceeding380 mg·g-1 at appropriate pH conditions imply the potential applications of nanocrystals in protein separation.
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