Investigations on the mechanism of the salt-induced peptide formation.
The applicability of the salt-induced peptide formation in aqueous solution--the simplest model so far for peptide synthesis under primitive earth conditions--is demonstrated for valine as another amino acid, and the formation of mixed peptides in systems containing glycine, alanine and valine is investigated. The dominant dipeptides formed are Gly-Gly, Gly-Ala and Gly-Val, at longer reaction times sequence inversion produces Ala-Gly and, considerably slower, Val-Gly. Ala-Ala is also produced and the relative amounts of the diastereomers prove the high conservation of optical purity of the original amino acids over a considerable time. The results lead to some further conclusions about the reaction mechanism and the possible dominance of peptide sequences in primordial dipeptides.
Schwendinger
M G
MG
Institute of Inorganic and Analytical Chemistry, University of Innsbruck, Austria.
Rode
B M
BM
D000409:Alanine / Q000138:chemical synthesis*; D000596:Amino Acids / Q000737:chemistry*; D003300:Copper / Q000737:chemistry*; D005998:Glycine / Q000138:chemical synthesis*; D008956:Models, Chemical; D010442:Peptide Chain Initiation, Translational; D010455:Peptides / Q000138:chemical synthesis*; D012965:Sodium Chloride / Q000737:chemistry*; D014633:Valine / Q000138:chemical synthesis*
D000596:Amino Acids; D010455:Peptides; D012965:Sodium Chloride; D003300:Copper; D014633:Valine; D000409:Alanine; D005998:Glycine