Investigations on the mechanism of the salt-induced peptide formation

Details Investigations on the mechanism of the salt-induced peptide formation Investigations on the mechanism of the salt-induced peptide formation

Nov 1992

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1992oleb...22..349s&link_type=abstract

Origins of Life and Evolution of the Biosphere, Volume 22, Issue 6, pp.349-359

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6

Scientific paper

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.

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