Journal of Guangxi Normal University(Natural Science Edition) ›› 2018, Vol. 36 ›› Issue (1): 105-111.doi: 10.16088/j.issn.1001-6600.2018.01.015

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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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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

CLC Number: 

  • O648
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