节点文献
中药有效成分盐酸小檗碱与胃蛋白酶相互作用及活性部位研究
Study on Interaction between Berberine Chloride and Pepsin and Location of the Active Groups during Binding Process
【作者】 豆妮娜; 李磊; 于芝颖; 赵可新; 刘雪锋; 赵英杰;
【Author】 DOU Ni-na;LI Lei;LIU Xue-feng;ZHAO Ying-jie;China National Petroleum Corporation Central Hospital;
【机构】 中国石油天然气集团公司中心医院; 北京大学人民医院; 江南大学化学与材料工程学院; 廊坊师范学院;
【摘要】 用荧光光谱(FS)、紫外光谱(UV)和核磁共振波谱(1H NMR)研究了中药有效成分盐酸小檗碱(BC)与胃蛋白酶(pepsin)之间的相互作用,探讨了BC与pepsin相互作用的机制和BC与pepsin结合的活性部位。结果表明:BC能够猝灭pepsin内源性荧光,且猝灭类型为静态猝灭;其结合常数(KA)为2.64×105dm3·mol-1(30℃)和1.66×105dm3·mol-1(37℃);BC与pepsin之间的相互作用为静电相互作用,且为自由能减少、熵驱动的过程,其结合距离为2.93nm(30℃)和2.90nm(37℃);BC能够插入pepsin分子内部,且BC与pepsin结合的关键部位位于BC分子的共轭π体系。
【Abstract】 The interaction between an active component of traditional Chinese Herb berberine chloride(BC) and pepsin has been studied by fluorescence, ultraviolet visible(UV-Vis) spectroscopy and 1 H-NMR. The mechanism of interaction between BC and pepsin and the active groups during BC-pepsin binding process were discussed. The results indicated that the endogenous fluorescence could be quenched by BC, and the quenching type was static quenching,;the association constants(KA) of BC-pepsin binding were 2.64× 105 dm3·mol-1(30℃) and 1.66×105 dm3·mol-1(37℃), respectively; The interaction force between BC and pepsin was electrostatic force, and the interaction process was driven by entropy changed along with free energy reduced. The distance between BC and pepsin were 2.93 nm(30℃) and 2.90 nm(37℃),respectively. BC could insert the pepsin molecule, and the active groups of BC binding pepsin were located on the conjugate π system.
- 【会议录名称】 2016年中国药学大会暨第十六届中国药师周论文集
- 【会议名称】2016年中国药学大会暨第十六届中国药师周
- 【会议时间】2016-12-08
- 【会议地点】中国北京
- 【分类号】R285
- 【主办单位】中国药学会