硫胺素及其修饰的CdSe量子点与血清蛋白相互作用的光谱法分析-分析化学专业论文.docxVIP

8 8 硫胺素及其修饰的 CdSe 量子点与血清蛋白相互作用的光谱法研究 the determination of VB1, and applied to the derermination of the real samples with satisfactory result. In chapter three, synthesis and characterization of VB1 capped CdSe QDs which is specially functional material for human body was investigated，this is used to achieve the surface modification of QDs by medicine and obtain special QDs. Experimental results found that VB1 capped QDs not only enhance biocompatibility but also make it stable greatly in aqueous solution. In chapter four, The interaction mechanism of bovine serum albumin (BSA) with VB1 capped CdSe QDs was studied using fluorescence quenching spectrum and Synchronous fluorescence spectrum in this chapter. The experimental results demonstrate that the quenching mechanism of BSA by VB1 capped CdSe QDs is static quenching, which was analysised by fluorescence spectroscopy and UV absorption spectroscopy. From thermodynamic coordination it can be confirmed that the binding force between VB1 capped CdSe QDs and BSA is mainly hydrogen bond and VDW(Van der Waals force). The effect of VB1 capped CdSe QDs on the conformation of BSA was analyzed by synchronous fluorescence spectrometry. In chapter five，The interaction mechanism of bovine serum albumin (BSA) with VB1 was studied using fluorescence quenching spectrum and Synchronous fluorescence spectrum in this chapter. The experimental results demonstrate that the quenching mechanism of BSA by VB1 is dynamic quenching, which was analysised by fluorescence spectroscopy and UV-vis. From thermodynamic coordination it can be confirmed that the binding force between VB1 and BSA is mainly hydrogen bond and VDW(Van der Waals force). The effect of VB1 on the conformation of BSA was analyzed by synchronous fluorescence spectrometry. Key Words：fluourescence spectroscopy；bovine serum albumin；thiamin；quantum dots 4 4 中南民族大学 学位论文原创性声明 本人郑重声明：所呈交的论文是本人在导师的指导下独立进行研究所取 得的研究成果。除了文中特别加以标注引用的内容外，本论文不包含任何其 他个人或集体已经发表或撰写的成果作品。对本文的研究做出重要贡献的个 人和集体，均已