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Citation: ZHAO Yufen. Discovery of Seryl-Histidine Dipeptide: From N-phosphoryl Amino Acids to Functional Dipeptides[J]. University Chemistry, ;2019, 34(12): 86-90. doi: 10.3866/PKU.DXHX201911044 shu

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

ZHAO Yufen ^1,2,

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 Date: 22 November 2019

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.
- Phosphorus,
- N-phosphoryl-amino acids,
- Seryl-histidine dipeptide
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