| Autor: |
Shu, Wanyun, Yu, Yongfei, Chen, Su, Yan, Xia, Liu, Yan, Zhao, Yufen |
| Zdroj: |
Origins of Life & Evolution of the Biosphere; Jun2018, Vol. 48 Issue 2, p213-222, 10p |
| Abstrakt: |
The Ser-His dipeptide is the shortest active peptide. This dipeptide not only hydrolyzes proteins and DNA but also catalyzes the formation of peptides and phosphodiester bonds. As a potential candidate for the prototype of modern hydrolase, Ser-His has attracted increasing attention. To explore if Ser-His could be obtained efficiently in the prebiotic condition, we investigated the reactions of N-DIPP-Ser with His or other amino acids in an aqueous system. We observed that N-DIPP-Ser incubated with His can form Ser-His more efficiently than with other amino acids. A synergistic effect involving the two side chains of Ser and His is presumed to be the critical factor for the selectivity of this specific peptide formation. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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