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

Biochem Biophys Res Commun. 2015 Oct 23;466(3):400-5. doi: 10.1016/j.bbrc.2015.09.038. Epub 2015 Sep 10.

Abstract

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.

Keywords: In vitro selection; Next-generation sequencing; Origin of proteins; Protein evolution; Structure and function; cDNA display.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / chemistry*
  • Amino Acids / chemistry*
  • Computational Biology
  • DNA, Complementary / metabolism
  • Gene Library
  • High-Throughput Nucleotide Sequencing
  • Hydrolysis
  • Ligands
  • Peptide Library*
  • Peptides / chemistry*
  • Prebiotics*
  • Protein Binding
  • Proteins / chemistry
  • RNA, Messenger / metabolism

Substances

  • Amino Acids
  • DNA, Complementary
  • Ligands
  • Peptide Library
  • Peptides
  • Prebiotics
  • Proteins
  • RNA, Messenger
  • Adenosine Triphosphate