A self-replicating peptide

Nature. 1996 Aug 8;382(6591):525-8. doi: 10.1038/382525a0.


The production of amino acids and their condensation to polypeptides under plausibly prebiotic conditions have long been known. But despite the central importance of molecular self-replication in the origin of life, the feasibility of peptide self-replication has not been established experimentally. Here we report an example of a self-replicating peptide. We show that a 32-residue alpha-helical peptide based on the leucine-zipper domain of the yeast transcription factor GCN4 can act autocatalytically in templating its own synthesis by accelerating the thioester-promoted amide-bond condensation of 15- and 17-residue fragments in neutral, dilute aqueous solutions. The self-replication process displays parabolic growth pattern with the initial rates of product formation correlating with the square-foot of initial template concentration.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Catalysis
  • DNA-Binding Proteins*
  • Fungal Proteins / chemistry*
  • Leucine Zippers
  • Molecular Sequence Data
  • Peptide Biosynthesis*
  • Peptides / chemistry
  • Protein Kinases / chemistry*
  • Saccharomyces cerevisiae Proteins*
  • Templates, Genetic
  • Transcription Factors / chemistry*


  • DNA-Binding Proteins
  • Fungal Proteins
  • Peptides
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Protein Kinases