An outstanding question in origins-of-life research is how polypeptides with structure and function arose from a complex soup of organics. Spark discharge reactions and meteorites suggest a vast array of amino acids and other species would have been present. Yet, there is often a disconnect between the accepted diversity of plausible monomers and those used to form abiotic peptides. We hypothesize the complexity of the primordial soup would have produced peptides and similar oligomers with diverse compositions, sequences, and structural motifs. Using mass spectrometry (MS) and infrared (IR) spectroscopy, we have been studying depsipeptides, or peptides with both amide and ester linkages, in this context. Depsipeptides form readily when mixtures of amino acids and hydroxy acids (e.g., lactic acid) are subjected to cycles of hydration and evaporation and their peptide character increases with repeated cycles. By varying amino and hydroxy acid monomers, we seek to gain insight into possible folding and/or catalysis at the polymer/peptide level.

Model primordial peptides with diverse monomer compositions, sequences, and structures

ACS Spring Meeting 2021

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