| 光谱法结合原子力显微镜研究呋喃唑酮与牛血清白蛋白的作用机理 |
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| 引用本文： | 张秋兰,逯露,李璋,倪永年. 光谱法结合原子力显微镜研究呋喃唑酮与牛血清白蛋白的作用机理[J]. 分析科学学报, 2017, 0(6): 752-756. DOI: 10.13526/j.issn.1006-6144.2017.06.002 |
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| 作者姓名： | 张秋兰 逯露 李璋 倪永年 |
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| 基金项目： | 国家自然科学基金，南昌大学食品科学与技术国家重点实验室基金 |
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| 摘 要： | 在人体生理(pH=7.4)条件下,应用荧光光谱和紫外光谱法研究药物呋喃唑酮与牛血清白蛋白(BSA)相互作用的机理,确定了呋喃唑酮对BSA的荧光猝灭机制。采用Stern-Volmer方程求出其相互作用的猝灭常数,并由双对数方程求出结合常数Ka和结合位点数n,采用热力学方法判别作用力类型。实验结果指出两者之间相互作用引起的荧光猝灭属静态方式,298K下结合常数Ka为6.50×106 L·mol~(-1),结合位点数n约为1,而作用力类型是氢键和范德华力。另外,还采用红外(IR)光谱、圆二色谱(CD)和原子力显微镜(AFM)研究了呋喃唑酮对BSA构象的影响。
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Spectroscopic Study on the Interaction Between Furazolidone with Bovine Serum Albumin |
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| Abstract: | The interaction between furazolidone (FZD) and bovine serum albumin (BSA) under simulative physiological conditions was investigated by various spectroscopies and AFM (atomic force microscopy) techniques.The experimental results indicated that the quenching mechanism of interaction of BSA with FZD was a static procedure.The negative values of △H(-16.22 kJ·mol-1) and △S(-26.01 J·mol-1 ·K 1) and the negative value of △G indicated that van der Waals force and hydrogen bonding interactions played major roles in the binding of FZD with BSA.The binding constant of FZD-BSA is 6.50× 106 L·mol 1 and the binding site is around one.The results of UV-Vis,FT-IR spectroscopy,CD (circular dichroism) and AFM showed that the binding of FZD to BSA induced the micro-environmental and conformational changes of BSA molecules. |
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