(582g) Peptide Hydrolysis and the Prebiotic Origin of Functional Peptides

The emergence of functional peptides under plausible prebiotic conditions has been an open scientific question for the origin of life on the prebiotic Earth around 4 billion years ago ^[1]. This research focuses on creating a one-pot system of peptides that is sufficiently simple to form spontaneously under prebiotic conditions, yet adequately complex to demonstrate functionality driven by selection. Hydrolysis of the amide bonds would drive the selection of short functional peptides. Here the function of these short peptides is demonstrated using the aldol reaction, in which glycline and proline based peptides can catalyze carbon-carbon bond formation ^[2] . The results demonstrate that the hydrolysis of oligomers back into monomers could replenish the limited monomer resources and reshuffle the peptide sequences. In this study, NMR analysis was performed to quantify the effects of temperature and pH on amide bond hydrolysis, starting from glycine and alanine containing oligomers. The rate constants are obtained by fitting differential equation models solved with MATLAB. The experimental data show that the amide bond hydrolysis is strongly impacted by pH, with hydrolysis promoted under more basic and higher temperature conditions.

References

1. Forsythe, J.G., et al., Ester‐Mediated Amide Bond Formation Driven by Wet–Dry Cycles: A Possible Path to Polypeptides on the Prebiotic Earth. Angewandte Chemie International Edition, 2015. 54(34): p. 9871-9875.
2. List, B., R.A. Lerner, and C.F. Barbas, Proline-catalyzed Direct Asymmetric Aldol Reactions. Journal of the American Chemical Society, 2000. 122(10): p. 2395-2396.