A self-replicating peptide.
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.
Lee
D H
DH
Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, USA.
Granja
J R
JR
Martinez
J A
JA
Severin
K
K
Ghadiri
M R
MR
D000595:Amino Acid Sequence; D002384:Catalysis; D004268:DNA-Binding Proteins; D005656:Fungal Proteins / Q000737:chemistry*; D016350:Leucine Zippers; D008969:Molecular Sequence Data; D010452:Peptide Biosynthesis; D010455:Peptides / Q000737:chemistry; D011494:Protein Kinases / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins; D013698:Templates, Genetic; D014157:Transcription Factors / Q000737:chemistry*
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D010455:Peptides; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D011494:Protein Kinases