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中国药学(英文版) ›› 2014, Vol. 23 ›› Issue (8): 543-547.DOI: 10.5246/jcps.2014.08.070

• 【研究论文】 • 上一篇    下一篇

绿原酸、新绿原酸、隐绿原酸与溶菌酶相互作用的荧光光谱法研究

兰月香, 刘梅仙, 陈世忠, 王弘*   

  1. 北京大学医学部 药学院 天然药物化学系, 北京 100191
  • 收稿日期:2014-05-07 修回日期:2014-05-14 出版日期:2014-08-31 发布日期:2014-05-27
  • 通讯作者: Tel./Fax: 86-10-82801559
  • 基金资助:
    Beijing Natural Science Foundation (Grant No. 7142088).

Spectrophotometric studies on the interaction between chlorogenic acid, neochlorogenic acid, cryptochlorogenic acid and lysozyme

Yuexiang Lan, Meixian Liu, Shizhong Chen, Hong Wang*   

  1. Department of Natural Medicines, School of Pharmaceutical Sciences, Peking University Health Science Center, Beijing 100191, China
  • Received:2014-05-07 Revised:2014-05-14 Online:2014-08-31 Published:2014-05-27
  • Contact: Tel./Fax: 86-10-82801559
  • Supported by:
    Beijing Natural Science Foundation (Grant No. 7142088).

摘要:

用荧光光谱法研究了绿原酸、新绿原酸、隐绿原酸与溶菌酶之间的相互作用。绿原酸(CA)、新绿原酸(NCA)、隐绿原酸(CCA)均能显著焠灭溶菌酶的内源荧光并以静态焠灭为主; 随着温度的升高其结合常数和结合位点均呈现降低的趋势。根据热力学参数判断确定CALYSO之间以疏水作用力为主, NCALYSO之间以氢键和范德力为主, CCALYSO之间以静电作用力为主。

关键词: 绿原酸, 新绿原酸, 隐绿原酸, 溶菌酶, 荧光光谱法

Abstract:

The interactions of chlorogenic acid (CA), neochlorogenic acid (NCA) and cryptochlorogenic acid (CCA) with lysozyme (LYSO) were investigated in physiological buffer by fluorescence spectroscopy. The mechanism study indicated that CA, NCA and CCA could strongly quench the intrinsic fluorescence of LYSO through static quenching procedures withone binding site. Thermodynamic data show that the major force in the binding processes of CA to LYSO was hydrophobicinteractions; for NCA, it was the hydrogen bonds and van der Waals forces, as for the CCA system, the mainly force is electrostatic force.

Key words: Chlorogenic acid, Neochlorogenic acid, Cryptochlorogenic acid, Lysozyme, Fluorescence quenching

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