酸抑制胰蛋白酶活性研究

单宁酸抑制胰蛋白酶活性研究单宁酸抑制胰蛋白酶活性研究摘 要作为由胰腺分泌的一种丝氨酸类的蛋白水解酶——胰蛋白酶，由于其价格低廉易提取，在众多领域发挥了其巨大作用。近几年来，针对胰蛋白酶抑制剂的有关研究也逐渐成为了热门方向，但目前针对具有抗氧化作用的单宁酸与胰蛋白酶研究形成的抑制剂在临床治疗方面的研究较少，本次论文则通过对胰蛋白酶结构分析得出能与单宁酸进行结合的胰蛋白酶活性位点区域，再与具有抗氧化作用等活性的单宁酸运用计算机软件进行分子动力学模拟运算得出单宁酸与胰蛋白酶两者结合时有关两者之间分子的几何构象偏差及其氢键数目变化，结合自由能计算出分子对接结合率，从而进一步论证得到单宁酸对胰蛋白酶的有较强的抑制作用，为后期进行有关单宁酸与胰蛋白酶催化活性实验提供理论支撑，对单宁酸-胰蛋白酶形成抑制剂在对人体康复有关治疗上贡献更多价值。关键词：胰蛋白酶抑制剂；分子对接计算；分子动力学；胰蛋白酶与单宁酸分子I动力学模拟；Study on the inhibition of trypsin activity by tannic acidAbstractAs a serine proteolytic enzyme secreted by the pancreas, trypsin plays an important role in many fields due to its low price and easy extraction. Of trypsin inhibitor in recent years, according to relevant research also gradually became the popular direction, but at present, in view of the antioxidant effect of tannic acid form and trypsin inhibitors in the clinical treatment of study is less, this thesis is through analyzing the structure of trypsin, this thesis is based on trypsin structure analysis can be combined with tannins trypsin activity site area, to have the activity such as antioxidant effect of tannic acid by using molecular dynamics simulation computer software operations between tannins and trypsin when a combination of the molecular geometry conformation of deviation, Combination of freedom to calculate the molecular docking rate, thus further argument for tannins have a stronger inhibitory effect of trypsin theory research, fo...