中文摘要：

用几种光谱方法研究了n C60纳米颗粒与牛血红蛋白之间的相互作用。用溶剂置换法制备n C60的水分散液,并用紫外-可见分光光度法、动态光散射和透射电子显微镜技术对n C60纳米颗粒进行表征;用紫外-可见分光光谱、荧光光谱、同步荧光光谱研究n C60与牛血红蛋白之间的作用。结果表明,n C60纳米颗粒对牛血红蛋白的紫外-可见吸收光谱有一定程度的改变作用;n C60可猝灭牛血红蛋白的内源荧光,且最大发射波长发生明显的蓝移现象;随着n C60浓度的增加,酪氨酸残基和色氨酸残基的同步荧光强度降低,其中酪氨酸残基峰位发生蓝移,而色氨酸残基峰位基本保持不变。研究表明n C60与牛血红蛋白之间存在一定的相互作用;n C60可引起牛血红蛋白构象的改变,酪氨酸残基所处微环境的极性减小,n C60与牛血红蛋白的作用位置更接近酪氨酸残基。

英文摘要：

Several spectroscopic methods were used to study the interaction between n C60 nanoparticles and bovine hemoglobin. The n C60 nanoparticles dispersion in water was prepared by solvent replacement method and characterized using UV-Vis spectrometry,dynamic light scattering and transmission electron microscopy. The interaction between n C60 and bovine hemoglobin was investigated by UV-Vis spectrometry,fluorescence spectroscopy and synchronous fluorescence spectroscopy. The result indicated that the UV-Visible absorption spectrum of bovine hemoglobin was changed to some extent by n C60 nanoparticles. The intrinsic fluorescence of bovine hemoglobin could be quenched by n C60 and the maximum emission wavelength showed obvious blue-shift. With the increasing concentrations of n C60,the synchronous fluorescence intensity of tyrosine and tryptophan residues decreased gradually,and the fluorescence peak of tyrosine residues exhibited a blue shift while the fluorescence peak of tryptophan residues remained unchanged. The research showed that the binding of n C60 to bovine hemoglobin could cause the conformation change of bovine hemoglobin. The microenvironment polarity around tyrosine residues decreased,indicating the binding site of n C60 to bovine hemoglobin was located near tyrosine residues.