The abiotic formation of peptides in water remains a fundamental challenge in origin-of-life research. Direct aqueous condensation of amino acids is thermodynamically hindered; consequently, existing models frequently depend on activation agents or require extreme conditions. We have developed and implemented an aqueous pathway for peptide synthesis mediated by carbamoyl phosphate (CAP) within a mild, “warm little pond” scenario. Co-incubation of diverse proteinogenic amino acids with CAP and metal cations promoted peptide bond formation. Our analysis reveals that magnesium ions operate synergistically with CAP, driving a dual-activation mechanism through
N
-carbamoylation and
O
-phosphorylation intermediates. Crucially, we establish that CAP can be generated in situ directly from early-Earth accessible precursors, urea and orthophosphate. This continuous aqueous pathway entirely bypasses the necessity for destructive dry-state cycles. CAP continues to play a vital role in nitrogen metabolism and the de novo synthesis of pyrimidine nucleotides in extant organisms. Therefore, we suggest that CAP serves as an evolutionary bridge, linking primordial geochemical conditions to the emergence of functional biochemical machinery.
Xiangxiao Zheng, Fude Chen, Min Zhang et al.· Communications Chemistry· 0 citations
A central question in origin-of-life research is how biological macromolecules and cellular structures arose from simple precursors under prebiotic conditions. This review focuses on the chemical evolution model of N-phosphoryl amino acids (NPAAs) and their multifaceted roles in this process. Featuring high-energy P–N bonds, NPAAs enable intramolecular activation via pentacoordinate phosphorus intermediates, facilitating the formation of homochiral peptides and nucleotides under mild aqueous conditions. Moreover, N-amino acid-nucleotide conjugates (N-aa-NMPs) drive peptide formation with chiral selection between amino acids and nucleosides, where the peptide yield for each amino acid is modulated by specific nucleosides, thereby laying a foundation for a proto-genetic code. Additionally, amphiphilic NPAA derivatives spontaneously self-assemble into vesicles and selectively condense peptides at membrane interfaces, whereas the in situ generation of N-fatty acyl amino acids further enhances membrane stability. Collectively, these findings support a phosphorus-centered model for the integrated origin of nucleic acids, proteins, and membranes.
Jianxi Ying, Yan Liu, Songsen Fu et al.· Accounts of Chemical Researc...· 0 citations
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