Orientation of the peptide formation of N-phosphoryl amino acids in solution |
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Authors: | Zhongzhou Chen Yufeng Tong Shuibing Chen Yanmei Li Yi Chen Yufen Zhao Jinfeng Wang |
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Institution: | (1) Bioorganic Phosphorus Chemistry Laboratory, Department of Chemistry, School of Life Science and Engineering, Tsinghua University, 00084 Beijing, China;(2) National Laboratory of Biomacromolecules, Center for Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, 100101 Beijing, China |
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Abstract: | The peptide formation of N-phosphoryl amino acids with amino acids proceeds in aqueous solution without any coupling reagents. After being separated
in sephadex gel column, the phosphoryl dipeptides were analyzed by the electrospray ionization tandem mass spectrometry (ESIMS/
MS). The result demonstrates that phosphoryl dipeptides were detected in all the reaction systems. It is found that the formation
of N-phosphoryl dipeptides is oriented: the N-terminal amino acid residues of the N-phosphoryl dipeptides are from N-phosphoryl amino acids, and the peptide elongation happened at the C-terminal. Only a-dipeptide, no β-dipeptide, is formed
in the N-phosphoryl dipeptides, showing that a-carboxylic group is activated selectively by N-phosphorylation. Theoretical calculation shows that the peptide formation of N-phosphoryl amino acids might happen through a penta-coordinate carboxylic-phosphoric intermediate in solution. These results
might give some clues to the study on the origin of proteins and protein biosynthesis. |
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Keywords: | N-phosphoryl amino acids orientation of peptide formation solution N-phosphoryl dipeptides |
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