广西师范大学学报（自然科学版） ›› 2018, Vol. 36 ›› Issue (1): 105-111.doi: 10.16088/j.issn.1001-6600.2018.01.015

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全氟两性表面活性剂与蛋白质相互作用研究

胡晓熙1,2,3,王芸1,2,文丰1,2,3,廖丹葵3,童张法3*   

  1. 1. 钦州学院石油与化工学院,广西钦州535099;
    2. 钦州学院广西高校北部湾石油天然气资源有效利用重点实验室,广西钦州535099;
    3. 广西大学化学化工学院,广西南宁530004
  • 收稿日期:2017-05-23 出版日期:2018-01-20 发布日期:2018-07-17
  • 通讯作者: 童张法(1963-),男,浙江慈溪人,广西大学教授,博士。E-mail:zhftong@sina.com
  • 基金资助:
    国家自然科学基金(51203082);广西高等学校优秀中青年骨干教师培养工程资助项目(GXQG022014064);中国博士后科学基金(2014M552287);广西高校化学工艺重点学科基金(2015KLOG16)

Interaction between Perfluorinated Amphiphilic Surfactant and Protein

HU Xiaoxi1,2,3,WANG Yun 1,2,WEN Feng1,2,3,LIAO Dankui3,TONG Zhangfa3*   

  1. 1.College of Petroleum and Chemical Engineering,Qinzhou University,Qinzhou Guangxi 535099,China;
    2. Guangxi Colleges and Universities Key Laboratory of Beibu Gulf Oil and Natural Gas Resource Effective Utilization, Qinzhou University,Qinzhou Guangxi 535099,China;
    3. College of Chemistry and Chemical Engineering, Guangxi University,Nanning Guangxi 530004,China
  • Received:2017-05-23 Online:2018-01-20 Published:2018-07-17

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摘要： 用荧光光谱法研究全氟烷基甜菜碱(PFAB)与牛血清白蛋白(BSA)的相互作用。结果表明:PFAB通过静态猝灭机理与BSA相互作用并使BSA荧光强度显著降低;298 K和310 K温度下,PFAB与BSA的结合常数分别为8.51×105和5.52×105 L/mol,结合位点数约为1,结合距离为1.93 nm;在PFAB和BSA的结合过程中静电力起主要作用;PFAB更倾向于与BSA中的色氨酸残基结合。

关键词: 全氟, 两性表面活性剂, 蛋白质, 荧光光谱法

Abstract: The interaction of perfluorinated alkyl betaine (PFAB) and bovine serum albumin (BSA) was studied mainly by fluorescent spectroscopy. The results show that PFAB can interact with BSA through a static quenching mechanism. The fluorescent intensity of BSA is dramatically quenched by PFAB. The binding constant of PFAB and BSA are 8.51×105 and 5.52×105 L/mol at 298 and 310 K, respectively. There is only one binding site with a binding distance is 1.93 nm. Electrostatic force plays a main role in the binding process of PFAB and BSA. It is more likely for PFAB to bind with tryptophan residue.

Key words: perfluorinated, amphiphilic surfactant, protein, fluorescence spectroscopy

中图分类号: 

  • O648
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