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依据阿维菌素与牛血清白蛋白的结合作用使牛血清白蛋白内源荧光发生改变的现象,用荧光光度法研究了在一定条件下阿维菌素和牛血清白蛋白相互作用的机理。结果表明,阿维菌素对牛血清白蛋白的荧光猝灭是形成了超分子化合物的静态猝灭过程。测定了在不同温度下阿维菌素与牛血清白蛋白的结合常数KA和结合位点数n分别为KA=2.26×103L·mol-1,n=1.08(25℃);KA=1.35×103L·mol-1,n=1.05(35℃)。根据阿维菌素与牛血清白蛋白相互作用的热力学参数,确定了阿维菌素与牛血清白蛋白之间的作用力类型为氢键和范德华力;根据Foerster非辐射能量转移理论求得阿维菌素与牛血清白蛋白的结合距离为2.55nm。用同步荧光光谱确定阿维菌素影响了BSA微区的构象。
The mechanism of the interaction between abamectin and bovine serum albumin was studied by fluorescence spectrophotometry under the condition of the change of endogenous fluorescence of bovine serum albumin by the combination of abamectin and bovine serum albumin. The results showed that the fluorescence quenching of bovine serum albumin by abamectin formed a static quenching process of supramolecular compounds. The binding constant KA and the number of binding sites n of abamectin and bovine serum albumin at different temperatures were determined as KA = 2.26 × 103L · mol-1, n = 1.08 (25 ℃); KA = 1.35 × 103L · mol-1, n = 1.05 (35 ° C). According to the thermodynamic parameters of the interaction between avermectin and bovine serum albumin, the type of force between avermectin and bovine serum albumin was determined as hydrogen bond and van der Waals forces; According to Foerster’s theory of non-radiative energy transfer The binding distance between the vitamins and bovine serum albumin is 2.55 nm. Simultaneous fluorescence spectroscopy was used to determine the effect of abamectin on the conformation of BSA microdomains.