ATP selection in a random peptide library consisting of prebiotic amino acids

Shou Kai Kang, Bai Xue Chen, Tian Tian, Xi Shuai Jia, Xin Yi Chu, Rong Liu, Peng Fei Dong, Qing Yong Yang, Hong Yu Zhang

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Based upon many theoretical findings on protein evolution, we proposed a ligand-selection model for the origin of proteins, in which the most ancient proteins originated from ATP selection in a pool of random peptides. To test this ligand-selection model, we constructed a random peptide library consisting of 15 types of prebiotic amino acids and then used cDNA display to perform six rounds of in vitro selection with ATP. By means of next-generation sequencing, the most prevalent sequence was defined. Biochemical and biophysical characterization of the selected peptide showed that it was stable and foldable and had ATP-hydrolysis activity as well.

Original languageEnglish
Pages (from-to)400-405
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - 23 Oct 2015
Externally publishedYes


  • In vitro selection
  • Next-generation sequencing
  • Origin of proteins
  • Protein evolution
  • Structure and function
  • cDNA display


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