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水热制备了约10 nm的CoFe2O4纳米晶,通过Zeta电势、动态光散射(Dynamic Light Scattering,DLS)和傅立叶变换红外光谱(FTIR)技术研究了纳米晶与牛血清白蛋白(Bovine Serum Albumin,BSA)和牛血红蛋白(Hemoglobin)的相互作用。纳米晶对BSA和血红蛋白都有很强的吸附,其中对血红蛋白的吸附符合静电吸附的规律,而对BSA的吸附则不符合静电吸附的规律。在pH=5.5和7.0时纳米晶对BSA和血红蛋白的吸附容量分别达到237.9 mg·g-1和256.9 mg·g-1。DLS结果表明蛋白质能够导致纳米晶团聚。吸附BSA或血红蛋白后,纳米晶的DLS粒径由51 nm分别增大到472 nm和114 nm。CoFe2O4纳米晶还导致了蛋白质FTIR谱发生明显变化。BSA和血红蛋白的酰胺I带由于纳米晶的作用分别减少了4 cm-1和6 cm-1。
The CoFe2O4 nanocrystals were prepared by hydrothermal method. The nanocrystals and Bovine Serum Albumin (BSA) were studied by Zeta potential, Dynamic Light Scattering (DLS) and Fourier Transform Infrared Spectroscopy (FTIR) ) And hemoglobin (Hemoglobin) interaction. Nanocrystals have a strong adsorption of BSA and hemoglobin, of which the adsorption of hemoglobin in line with the law of electrostatic adsorption, while the adsorption of BSA is not consistent with the law of electrostatic adsorption. The adsorption capacity of BSA and hemoglobin to nanocrystals reached 237.9 mg · g-1 and 256.9 mg · g-1, respectively at pH = 5.5 and 7.0. DLS results show that the protein can cause nanocrystal agglomeration. After adsorbing BSA or hemoglobin, the particle size of nanocrystalline DLS increased from 51 nm to 472 nm and 114 nm, respectively. CoFe2O4 nanocrystals also led to significant changes in FTIR spectra. Amide I bands of BSA and hemoglobin were reduced by 4 cm-1 and 6 cm-1, respectively, due to the nanocrystalline effect.