高等学校化学学报

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芘与人血清白蛋白和牛血清白蛋白结合位点微环境极性的差异

李梦硕1, 张静2, 刘丹1, 朱亚先3, 张勇1()   

  1. 1.近海海洋环境科学国家重点实验室(厦门大学), 厦门大学环境与生态学院, 厦门 361000
    2.河口生态安全与环境健康省重点实验室, 厦门大学嘉庚学院, 漳州 363105
    3.厦门大学化学化工学院化学系, 厦门 361005
  • 收稿日期:2020-08-13
  • 通讯作者: 张勇 E-mail:yzhang@xmu.edu.cn
  • 基金资助:
    国家自然科学基金委重大科研仪器研制项目(21627814)

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 Enviro nmental 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
  • Contact: ZHANG Yong E-mail:yzhang@xmu.edu.cn
  • Supported by:
    ? Supported by the National Natural Science Foundation of China(21627814)

摘要:

利用芘(Pyr)的微环境极性探针性质, 采用稳态荧光光谱、 荧光共振能量转移技术结合分子对接法, 对比分析了Pyr分别与人血清白蛋白(HSA)和牛血清白蛋白(BSA)作用机制的差异. 结果表明, HSA和BSA中Pyr的I1/I3平均值分别为1.36和0.92; Pyr与HSA和BSA的结合常数分别为1.86×107和1.71×105 L/mol; Pyr与HSA和BSA中色氨酸残基表观距离分别为2.37和2.34 nm. Pyr在HSA和BSA中不同的结合位点位于ⅠB子域和ⅠA子域, 其结合位点周围氨基酸残基的极性是影响Pyr I1/I3值的主要原因之一. 实验证实Pyr与HSA和BSA结合作用位点处的微环境极性存在差异.

关键词: 芘, 人血清白蛋白, 牛血清白蛋白, 微环境极性, 相互作用机制

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/molto 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(Ed.: N, K)

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