Acta Phys. -Chim. Sin. ›› 2014, Vol. 30 ›› Issue (7): 1239-1246.doi: 10.3866/PKU.WHXB201405151

• THEORETICAL AND COMPUTATIONAL CHEMISTRY • Previous Articles     Next Articles

Interactions between Trehalose and Amino Acids by Molecular Dynamics Simulations

BAI Shu1,2, CHANG Ying1, LIU Xiao-Juan1, LIU Fu-Feng1,2   

  1. 1. Key Laboratory of Systems Bioengineering of the Ministry of Education, Department of Biochemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, P. R. China;
    2. Collaborative Innovation Center of Chemical Science and Engineering Tianjin, Tianjin 300072, P. R. China
  • Received:2014-03-04 Revised:2014-05-14 Published:2014-06-30
  • Contact: LIU Fu-Feng E-mail:fufengliu@tju.edu.cn
  • Supported by:

    The project was supported by the National Natural Science Foundation of China (20906068) and China Postdoctoral Science Foundation (2013M530115, 2012T50241).

Abstract:

Although trehalose is used as a protein stabilizer, the mechanism by which this stability is induced is not fully understood at present. In this study, we investigated the interactions between trehalose and all 20 common amino acids using all-atom molecular dynamics simulations. It is found that all the amino acids exhibit a preference for contact with water, especially the polar and charged amino acids. Conversely, only the hydrophobic amino acids were found to have a slight preference for contact with trehalose molecules. This tendency is most pronounced in the case of contact between trehalose and aromatic or hydrophobic side chains, whereas the backbones of each amino acids all show similar propensities for contact with water. Furthermore, hydrogen bonds between amino acids and trehalose were found to be significantly weaker than those between amino acids and water, although both trehalose and water can interact with the amino acids via hydrogen bonds. These findings are important with regard to the exploration of the molecular mechanism of protein stability induced by trehalose and the rational design of highly efficient protein stabilizers.

Key words: Trehalose, Osmolyte, Molecular dynamics simulation, Protein stability, Hydrogen bond

MSC2000: 

  • O641