University Chemistry ›› 2019, Vol. 34 ›› Issue (12): 86-90.doi: 10.3866/PKU.DXHX201911044

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Discovery of Seryl-Histidine Dipeptide: From N-phosphoryl Amino Acids to Functional Dipeptides

Yufen ZHAO1,2,*()   

  1. 1 College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, Fujian Province, P. R. China
    2 Institute of Drug Discovery Technology, Ningbo University, Ningbo 315211, Zhejiang Province, P. R. China
  • Received:2019-11-22 Accepted:2019-11-25 Published:2019-12-09
  • Contact: Yufen ZHAO
  • Supported by:


Phosphorus is one of the important elements for life, which participates in various biochemical processes. L-Amino acids are the basic structural units of proteins. N-phosphorylation of amino acids makes them be activated and become one kind of "micro activating enzyme", which possesses a variety of biochemical reaction activities, such as peptide formation. Based on the peptide formation reaction of N-phosphoryl amino acids, L-seryl-L-histidine dipeptide (Seryl-histidine dipeptide) is produced and found that it is the smallest functional peptide with a variety of biological enzyme activities. Seryl-histidine dipeptide could be regarded as the original evolution prototype of modern hydrolytic enzyme. This paper reviews the research process from N-phosphoryl amino acids to the discovery of seryl-histidine dipeptide in detail. There are pain, confusion and joy, which fully embodies the charm of scientific exploration.

Key words: Phosphorus, N-phosphoryl-amino acids, Seryl-histidine dipeptide