刘里, 成飞翔. 光谱法研究泮托拉唑钠与牛血清白蛋白的相互作用[J]. 华南师范大学学报(自然科学版), 2017, 49(1): 74-79.
引用本文: 刘里, 成飞翔. 光谱法研究泮托拉唑钠与牛血清白蛋白的相互作用[J]. 华南师范大学学报(自然科学版), 2017, 49(1): 74-79.
LIU L, CHENG F X. Study on the Interaction between Pantoprazole Sodium and Bovine Serum Albumin by Spectrometry[J]. Journal of South China Normal University (Natural Science Edition), 2017, 49(1): 74-79.
Citation: LIU L, CHENG F X. Study on the Interaction between Pantoprazole Sodium and Bovine Serum Albumin by Spectrometry[J]. Journal of South China Normal University (Natural Science Edition), 2017, 49(1): 74-79.

光谱法研究泮托拉唑钠与牛血清白蛋白的相互作用

Study on the Interaction between Pantoprazole Sodium and Bovine Serum Albumin by Spectrometry

  • 摘要: 在优化的实验条件下,运用荧光光谱法和紫外光谱法研究牛血清白蛋白(BSA) 与泮托拉唑钠(PS)的结合作用。研究表明:PS对BSA的荧光有猝灭作用,属于静态猝灭。BSA能运载PS,是一个自发过程,其作用力类型主要为氢键和范德华力。BSA 的亚螺旋域ⅢA是主要结合位置,离酪氨酸残基更近,有正协同作用。PS对BSA构象产生影响,使BSA腔内疏水环境的极性减弱。该实验对揭示药物动力学问题及后续抗菌类药物的研发提供了理论依据。

     

    Abstract: Under the optimal conditions,the interaction of Pantoprazole Sodium(PS) with bovine serum albumin(BSA) was investigated by fluorescence spectrometry and ultraviolet-visible light absorption spectrometry. It showed that the fluorescence of BSA was quenched by PS, which was a static quenching process. BSA could transport PS. It was spontaneous and mainly driven by hydrogen bond and Vander Waals force. The primary binding site for PS was located at sub-domain ⅡA of BSA and near by tyrosine residue. There was some positive cooperative effect. The conjugation reaction would affect the conformation of BSA, leading to the polarity around BSA weakened. This test provided a theoretical basis for revealing the pharmacokinetics and further research on development of new antibacterial drugs.

     

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