Accelerated peptide bond formation at air-water interfaces.

ABSTRACT: Peptides and proteins, essential components of living organisms, are composed of amino acids linked by peptide bonds. However, the mechanism of peptide bond formation during the prebiotic era remains unclear. In this study, advanced Born-Oppenheimer molecular dynamics (BOMD) simulations were used to investigate the mechanisms and kinetics of peptide bond formation at air-water interfaces using diglycine, the simplest dipeptide, as a model molecule. The results show that peptide bonds can be rapidly formed via a unique isomerization-then-OH^--elimination pathway. In this mechanism, the diglycine initially isomerizes into its acidic form at the air-water interface, followed by a reaction that releases an OH^- anion rather than the previously hypothesized H₂O. T

SUBMITTER: Xia D 

PROVIDER: S-EPMC11962484 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature