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 in...

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Bibliographic Details
Published in:Origins of life and evolution of biospheres 1992-11, Vol.22 (6), p.349-359
Main Authors: Schwendinger, M G, Rode, B M
Format: Article
Language:English
Subjects:
Alanine - chemical synthesis
Amino Acids - chemistry
Copper - chemistry
Glycine - chemical synthesis
Models, Chemical
Peptide Chain Initiation, Translational
Peptides - chemical synthesis
Sodium Chloride - chemistry
Space life sciences
Valine - chemical synthesis
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Summary: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.
ISSN:0169-6149
1573-0875
DOI:10.1007/bf01809371