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化学学报
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化学学报 ›› 2011, Vol. 69 ›› Issue (02): 190-198. 上一篇    下一篇

研究论文

Fe3＋存在下磺胺甲恶唑与牛血清白蛋白相互作用的光谱学研究

余燕敏1，冯金朝1，刘颖*,1,2   

  1. (1中央民族大学生命与环境科学学院 北京 100081)
    (2内蒙古师范大学化学与环境科学学院 呼和浩特 010022)
  • 投稿日期:2010-07-09 修回日期:2010-09-08 发布日期:2010-09-20
  • 通讯作者: 刘颖 E-mail:liuying430@yahoo.com.cn
  • 基金资助:

    国家自然科学基金项目;国家民委科研项目;中央民族大学“985工程”项目;中央民族大学“211工程”项目;中央民族大学2009-2010年度自主科研计划项目;中央民族大学2009年度研究生“自主科研项目”

Spectroscopic Study of the Interaction between Sulfamethoxazole and Bovine Serum Albumin in the Presence of Fe3＋

Yu Yanmin1 Feng Jinchao1 Liu Ying*,1,2   

  1. (1 College of Life and Environmental Science, Minzu University of China, Beijing 100081)
    (2 Inner Mongolia Normal University, Huhhot 010022)
  • Received:2010-07-09 Revised:2010-09-08 Published:2010-09-20
  • Contact: Ying LIU E-mail:liuying430@yahoo.com.cn

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在模拟生理条件下, 应用荧光光谱、紫外吸收光谱以及傅立叶变换红外光谱研究Fe3＋存在下磺胺甲恶唑(Sulfamethoxazole, SMZ)与牛血清白蛋白(Bovine Serum Albumin, BSA)的相互作用. 结果表明, Fe3＋存在时SMZ与BSA结合常数增大, 作用力类型由疏水作用力转变为氢键和范德华力. 无论Fe3＋存在与否, SMZ与BSA之间作用机制均为静态荧光猝灭. 同步荧光及三维荧光光谱表明, SMZ改变了BSA构象, Fe3＋的存在没有加强SMZ对BSA有序结构的改变. 从紫外吸收光谱可知, Fe3＋先与SMZ形成配合物后再与BSA形成三元复合物. 根据非辐射能量转移理论, 求出结合位置与212位色氨酸残基距离. FT-IR光谱显示, Fe3＋存在时SMZ对BSA二级结构的变化产生不同的影响.

关键词: 牛血清白蛋白, 磺胺甲恶唑, Fe3＋, 荧光光谱, 紫外吸收光谱, 傅立叶红外光谱

Under the simulative human physiological condition, the interaction of sulfamethoxazole (SMZ) and bovine serum albumin (BSA) with or without Fe3＋ was studied by fluorescence spectra, ultra-violet absorption spectra and FT-IR spectra. The results show that both the quenching mechanism of the intrinsic fluorescence of BSA by sulfamethoxazole with or without Fe3＋ is a static fluorescence quenching procedure. It was found that in the presence of Fe3＋, the binding constant of SMZ and BSA increased and the main binding force between SMZ and BSA was changed from hydrophobic force to hydrogen bonds and van der Waals force. From the synchronous fluorescence and three-dimensional fluorescence spectra, it was found that SMZ change the conformation of BSA. BSA may form a new disordered structure, but the capability of SMZ changing the structure of the BSA was not enhanced in the presence of Fe3＋. Based on fluorescence resonance energy transfer (FRET), the distances (r) between donor (BSA) and acceptor (SMZ and Fe3＋-SMZ) were obtained. According to FT-IR, the secondary structure of BSA changed when Fe3＋ and SMZ were added.

Key words: bovine serum albumin, sulfamethoxazole, Fe3＋, fluorescence spectroscopy, UV absorption spectra, Fourier transform infrared spectroscopy

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