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利用荧光光谱法与分子对接模拟计算系统地研究了吴茱萸次碱同牛血清白蛋白及人血清白蛋白间相互作用情况。荧光光谱实验结果表明,在37℃及生理p H条件下的水溶液中,吴茱萸次碱可以有效地猝灭牛血清白蛋白与人血清白蛋白的荧光发射。根据Stem-Volmer方程及双对数方程计算可知,吴茱萸次碱对牛血清蛋白与人血清白蛋白的荧光猝灭均为静态猝灭,吴茱萸次碱可以同这两种蛋白质形成1:1型稳定的复合物。采用了恒波长同步荧光法研究了吴茱萸次碱与这两种血清蛋白可能的结合位点,并且通过分子对接模拟计算方法推测了吴茱萸次碱与这两种血清蛋白可能的结合模型,结果表明,吴茱萸次碱与血清蛋白最有可能的结合位点为Trp213残基(牛血清白蛋白)或Trp214残基(人血清白蛋白)附近。
The interaction between rutaecarpine and bovine serum albumin (BSA) and human serum albumin (BSA) was studied systematically using fluorescence spectroscopy and molecular docking simulation. The results of fluorescence spectroscopy showed that rutaecarpine effectively quenched the fluorescence emission of bovine serum albumin and human serum albumin in aqueous solution at 37 ℃ and physiological pH. According to Stem-Volmer equation and double logarithm equation, the fluorescence quenching of rutin and bovine serum albumin is statically quenched by rutaecarpine, and rutaecarpine can form a stable 1: 1 type with these two proteins Complex. The possible binding sites of rutaecarpine and the two serum proteins were studied by the method of constant-wavelength synchronous fluorescence and the possible binding model between rutaecarpine and the two serum proteins was inferred by the molecular docking simulation method. The most likely site of binding of rutaecarpine to serum proteins is near Trp213 residues (bovine serum albumin) or Trp214 residues (human serum albumin).