An outstanding question in origins-of-life research is how functional polypeptides arose from a complex soup of organics. Both spark discharge reactions and meteorites suggest a vast array of small monomers would have been present and in significant abundances. Yet there is often a disconnect between the accepted diversity of plausible monomers and those used to form peptides in model prebiotic reactions. Indeed, the majority of studies on proto-peptide formation use only the simplest amino acid monomers, glycine and/or L-alanine. In contrast, we in the Center for Chemical Evolution hypothesize that the complexity of the prebiotic soup would have produced proto-peptides with a broader scope of compositions, sequences, and structural motifs. Using infrared (IR) spectroscopy and mass spectrometry (MS) techniques, we have been studying proto-peptides with both traditional alpha-amino acid monomers (glycine, L-alanine, L-valine, etc.) and non-canonical monomers such as beta-amino acids, alpha-hydroxy acids, or D-amino acids. Such proto-peptides are quite challenging from an analytical point of view, but we feel our efforts are worthwhile as (1) diverse compositions and sequences were likely more realistic in prebiotic scenarios; (2) various monomers could have lowered the activation barrier for polypeptide formation and/or stabilization; and (3) studying the roles of various monomers could suggest potential causes for biological selection of the 20 canonical amino acids found in ribosomal polypeptides.

Embracing the complexity of the prebiotic soup: Proto-peptides with diverse monomer compositions and sequences

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.