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Preparation of Fe-based Nanomaterials and the Interactions with Proteins

Author: LiQiang
Tutor: HuangXinTang
School: Central China Normal University
Course: Condensed Matter Physics
Keywords: Ferrite nanocrystals α-Fe2O3nanostructures BSA Hemoglobin Interaction
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Type: PhD thesis
Year: 2014
Downloads: 5
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Abstract


Interaction with protein is a key factor determining the biological responses to nanomaterials, including biological toxicity, biocompatibility, cellular recognization, cellular uptake etc. When nanomaterials are exposed to biological medium, the interactions with protein will lead a "protein corona" covering on the surface of nanomaterials. This protein corona will modify the biological identity and make the biological behavior different to the nanomaterials itself. For this reason, protein-nanomaterial interaction is an important biological propety which should be understood in order to evaluate nanomaterial biocompatibility or biosafety. In the nanobiotechnology field, nanomaterials have potential to be applied in drug delivery, genic carrier, protein purification as well as biosensor etc. In this case, protein-nanomaterial interactions will significantly affect the performance of nanomaterials. Therefore, the applications of nanomaterials in biological field also require the knowledge on protein-nanomaterial interaction.Iron oxides nanostructures have potential applications in biotechnology field that including magnetic drug carrier, hyperthermia application, MRI contrast agent and protein separation etc. In order to extend the biological applications of iron oxides nanostructures, the interactions with protein and the associated mechanism should be investigated. For above mentioned viewpoint, this thesis focuses on protein interaction behaviors of two class of important iron oxides nanomaterials-ferrite and hematite. The main works are detailed as follows:1. Ferrite nanocrystals NiFe2O4, CoFe2O4, ZnFe2O4and Nio.5Co0.5Fe2O4were prepared by hydrothermal method. Stoichiometric reagents were first dissolved in water, then co-preciptate by ammonia water. The colloid precipitation was hydrothermally treated at190℃for10hours. The obtained products were spherical nanocrystal with diameter about10nm. XRD analysis confirmed that all the products were spinel crystalline structure. The EDX analysis indicated that the elemental contents were consistent with the formula NiFe2O4, CoFe2O4, ZnFe2O4and Nio.5Coo.5Fe2O4. Specific area of nanocrystals was determined by BET method. The results showed that the BET of nanocrystals approximated to their theoretical values.2. The mechanism on protein adsorption to ferrite nanocrystals were investigated by Zeta potential technology. Adsorption behaviors between BSA and four nanocrystals can not be attributed to electrostatic interactions. Hemoglobin adsorbed to NiFe2O4, CoFe2O4and ZnFe2O4nanocrystals via electrostatic interactions. But, the adsorption between hemoglobin and Ni0.5Co0.5Fe2O4was not consistent with electrostatic interactions. Protein adsorption can lead to nanocrystals aggregation, which has been detected by Dynamic Light Scattering (DLS) technique. FTIR showed that protein conformation had been changed due to the nanocrystal-protein interactions.3. Different morphological α-Fe2O3nanostructures were prepared by hydrothermal method. Under the mediation of sodium acetate, α-Fe2O3hierarchical microsphere and α-Fe2O3nanoparticle can be obtained. Hydrothermal method was also applied to prepare Ti4+doped α-Fe2O3nanoparticles. All the products were analysis by N2adsorption-desorption experiment and the BET values were acquired. Results showed that α-Fe2O3nanoparticle possessed higher specific area than hierarchical microsphere morphology. The Ti4+dopant had very little impact on the specific area of α-Fe2O3nanoparticles.4. Morphology had significant impact on protein adsorption behaviors of α-Fe2O3nanostructures. All the hierarchical α-Fe2O3microspheres had no ability to adsorb BSA or hemoglobin. Only α-Fe2O3nanoparticles can adsorb BSA and hemoglobin with high capacity. Zeta potential measurements indicated that adsorption mechanism can not be expalined by electrastatic interactions. Ti4+doping was another factor determining protein adsorption behaviors of α-Fe2O3nanoparticles. The doped nanoparticles only adsorbed BSA and hemoglobin under ultrasonic irradiation. Without ultrasonication assisted, Ti4+doped α-Fe2O3nanoparticles completely lost the ability to adsorb protein. On the contrary, pure α-Fe2O3nanoparticles can directly adsorb protein irrelevant to ultrasonic treatment. In addition, the protein adsorption capacity of Ti4+doped α-Fe2O3nanoparticles was much higher than that of undoped counterpart.

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