【摘要】 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。更多还原

【Abstract】 Cobalt ferrite(CoFe2O4) nanocrystals(approximately 10 nm) were prepared by hydrothermal method and their interactions with Bovine Serum Albumin(BSA) and bovine hemoglobin were investigated by Zeta potential, Dynamic Light Scattering(DLS) and FTIR Spectroscopy techniques. Results show that nanocrystalhemoglobin adsorption correlates to electrostatic attractive/repulsive interaction, whereas BSA does not follow this scheme. The corresponding adsorption capacity of BSA and hemoglobin reaches a maximum value of 237.9 mg·g-1and 256.9 mg·g-1at pH value of 5.5 and 7.0, respectively. DLS measurements indicate that protein adsorption have led to nanocrystal-protein aggregates formation. Comparing to the hydrodynamic size of bare nanocrystals(51 nm), that for BSA and hemoglobin increases to 472 nm and 114 nm respectively upon protein adsorption. The interaction with nanocrystal also induces protein conformation changes. The amide I band in IR spectrum shifts4 cm-1and 6 cm-1, respectively, to lower wavenumbers in the case of BSA and hemoglobin.更多还原