荧光光谱法研究灯盏花素与牛血清白蛋白相互作用 - 中国现代应用药学.pdf

荧光光谱法研究灯盏花素与牛血清白蛋白相互作用 高平章，吴洪，郭婧，许亚妹(泉州师范学院化学与生命科学学院，福建 泉州 362000) 摘要：目的 采用荧光光谱法研究灯盏花素与牛血清白蛋白(BSA)在生理条件下(pH 7.4)的相互作用机制。方法 固定BSA 浓度，依次加入不同浓度的灯盏花素溶液，在激发波长为280 nm 下，290~500 nm 的波长范围内进行荧光猝灭光谱、同 步荧光光谱扫描。结果 灯盏花素对BSA 的荧光猝灭类型是静态猝灭；在温度288 K 和310 K 时，二者的结合常数KA 分别为8.295×105 和3.302×105 L·mol1 ；二者的结合位点数n 分别为 1.239 3 和 1.177 0。由热力学参数焓变(ΔH= 31.080 kJ·mol1) 小于零和熵变(ΔS=5.392 J·mol1·K1) 大于零，确定灯盏花素与BSA 之间的作用力类型为静电作用力；生成自由能 变(ΔG)为负值，表明灯盏花素与BSA 的作用过程是一个自发过程。此外，应用同步荧光光谱考察了灯盏花素对BSA 构 象的影响。结论 经过荧光光谱分析，可以确定灯盏花素与白蛋白的作用机制，为其开发成治疗心血管疾病新药提供理 论依据。 关键词：灯盏花素；牛血清白蛋白；荧光光谱法；相互作用 中图分类号：R962.1 文献标志码：A 文章编号：1007-7693(2012)02-0106-04 Study on the Interaction between Breviscapinum and Bovine Serum Albumin by Fluorescence Spectrometry GAO Pingzhang, WU Hong, GUO Jing, XU Yamei(College of Chemistry and Life Science, Quanzhou Normal University, Quanzhou 362000, China) ABSTRACT: OBJECTIVE To identify the interaction mechanism between breviscapinum and bovine serum albumin(BSA) under the physiological conditions (pH 7.4) by fluorescence spectrometry. METHODS Fixing the concentration of BSA, different concentrations of breviscapinum were added. At excitation wavelength 280 nm, the interaction between breviscapinum and BSA was determined with quenching and synchronous spectrum from 290 nm to 500 nm. RESULTS The fluorescence quenching mechanism between breviscapinum and BSA was static quenching. The binding constants (KA ) under 288 K and 310 K between breviscapinum and BSA were 8.295×105 and 3.302×105 L·mol1, respectively. The number of binding sites under 288 K and 310 K between breviscapinum and BSA were 1.239 3 and 1.177 0, respectively. According to the thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS), which were calculated to be 31.080 kJ·mol1 and 5.392 J·mol1·K1, r