高等学校化学学报 ›› 2015, Vol. 36 ›› Issue (5): 881-885.doi: 10.7503/cjcu20141037

• 分析化学 • 上一篇    下一篇

基于表面等离子体共振技术的血清白蛋白与色氨酸对映异构体手性识别的热力学研究

申刚义1(), 高妍1, 张爱芹2, 崔箭1, 戴东升3()   

  1. 1. 中央民族大学中国少数民族传统医学研究院
    2. 生命与环境科学学院, 北京100081
    3. 太原琳焓达科技有限公司, 太原 044602
  • 收稿日期:2014-11-25 出版日期:2015-05-10 发布日期:2015-03-31
  • 作者简介:联系人简介: 申刚义, 男, 博士, 副研究员, 主要从事民族医药分析新方法研究. E-mail: shengy@muc.edu.cn; 戴东升, 男, 博士, 高级工程师, 主要从事生物制药研究. E-mail: dongshengdai@126.com
  • 基金资助:
    国家自然科学基金(批准号: 81001595)、 国家民族事务委员会科研项目(批准号: 14ZYZ018)和长江学者和创新团队发展计划项目(批准号: IRT_13R63)资助

Thermodynamic Study of Chiral Recognition Between Serum Albumin and Tryptophan Enantiomers by Surface Plasmon Resonance

SHEN Gangyi1,*(), GAO Yan1, ZHANG Aiqin2, CUI Jian1, DAI Dongsheng3,*()   

  1. 1. Institute of Chinese Minority Traditional Medicine
    2. College of Life and Environmental Science, Minzu University of China, Beijing 100081, China
    3. Taiyuan Linhanda Technology Co., Ltd., Taiyuan 044602, China
  • Received:2014-11-25 Online:2015-05-10 Published:2015-03-31
  • Contact: SHEN Gangyi,DAI Dongsheng E-mail:shengy@muc.edu.cn;dongshengdai@126.com
  • Supported by:
    † Supported by the National Natural Science Foundation of China(No.81001595), the State Ethnic Affairs Commission Foundation of China(No.0910KEQN67) and the Program for Changjiang Scholars and Innovative Research Team in University of China(No.IRT_13R63)

摘要:

利用表面等离子体共振(SPR)技术, 从热力学角度研究了牛血清白蛋白、 人血清白蛋白与色氨酸对映异构体相互作用的手性识别, 考察了pH值、 离子强度和温度对亲和力的影响. 利用热力学方法计算并探讨了作用机理. 实验结果表明, 牛血清白蛋白及人血清白蛋白与L-色氨酸的结合有高度特异性. 热力学参数计算结果证明疏水作用在手性识别过程中起主要作用, 但不排除静电作用有一定的贡献.

关键词: 表面等离子体共振, 手性识别, 血清白蛋白, 色氨酸, 热力学

Abstract:

The chiral recognition between serum albumin and L-/D-tryptophan was studied by surface plasmon resonance from the point of view of thermodynamic. The effects of pH, ionic strength of buffer solution and temperature on binding affinity were investigated in detail. The thermodynamic parameters were further evaluated and used to explore the chiral recognition mechanism. It has been found that both BSA and HSA had excellent chiral recognition capability to L- and D-tryptophan. Moreover, there were highly specific interactions between BSA(HSA) and L-tryptophan in comparison with D-tryptophan. The calculated results of thermodynamic parameters indicated that the hydrophobic interaction played a dominant role. In addition, electrostatic interaction may also certainly contribute to the interactions between L-tryptophan and serum albumin.

Key words: Surface plasmon resonance, Chiral recognition, Serum albumin, Tryptophan, Thermodynamic

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