Chem. J. Chinese Universities ›› 2015, Vol. 36 ›› Issue (5): 881.doi: 10.7503/cjcu20141037

• Analytical Chemistry • Previous Articles     Next Articles

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)

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

CLC Number: 

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