Chem. J. Chinese Universities ›› 2021, Vol. 42 ›› Issue (3): 731.doi: 10.7503/cjcu20200559

• Analytical Chemistry • Previous Articles     Next Articles

Interactions of Pyrene with Human Serum Albumin and Bovine Serum Albumin: Microenvironmental Polarity Differences at Binding Sites

LI Mengshuo1, ZHANG Jing2, LIU Dan1, ZHU Yaxian3, ZHANG Yong1()   

  1. 1.State Key Laboratory of Marine Environmental Sciences of China (Xiamen University),College of Environment and Ecology,Xiamen University,Xiamen 361102,China
    2.Key Laboratory of Estuarine Ecological Security and Environmental Health,Tan Kah Kee College,Xiamen University,Zhangzhou 363105,China
    3.College of Chemistry and Chemical Engineering,Xiamen University,Xiamen 361005,China
  • Received:2020-08-13 Online:2021-03-10 Published:2021-03-08
  • Contact: ZHANG Yong E-mail:yzhang@xmu.edu.cn
  • Supported by:
    ? Supported by the National Natural Science Foundation of China(21627814)

Abstract:

The interactions of pyrene(Pyr), a microenvironmental hydrophobic fluorescent probe, with human serum albumin(HSA) or bovine serum albumin(BSA) were investigated using steady-state fluorescence, fluorescence resonance energy transfer technology, and molecular docking methods. It was observed that the average values of I1/I3 of the Pyr in the presence of HSA or BSA are 1.36 and 0.92, respectively. The binding constants of Pyr with HSA or BSA has been decreased from 1.86×107 L/mol to 1.71×105 L/mol. The apparent distances of Pyr to tryptophan residues in HSA or BSA were calculated to be 2.37 and 2.34 nm. The binding sites of Pyr in HSA or BSA were located in subdomain ⅠB and subdomains ⅠA, respectively. The polarity of amino acid residues around the binding sites was one of the main factors affecting the I1/I3 value of Pyr. The experimental results suggested that there were significant differences in the binding sites and its microenvironmental polarity of BSA and HSA with Pyr.

Key words: Pyrene, Human serum albumin, Bovine serum albumin, Microenvironmental polarity, Interaction mechanism

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