Light-Driven Competitive Selection in a Protein-Catalyzed Dissipative Peptide Replication

Theoretical models of prebiotic evolution propose that catalytic modulation can influence autocatalytic replication cycles. We hypothesized that a protein catalyst could create a favorable environment for proximity-controlled, dissipative replication of primitive peptides. This setup, in principle, allows competitive selection by making the catalyst a limited resource. Here, we show that a structurally flexible and promiscuous protein, calmodulin, catalyzes UVA light-driven replication in a helical foldamer-based replicator system. The protein accelerates both non-autocatalytic synthesis and autocatalytic replication, with autocatalysis being the dominant pathway. The system demonstrates light-intensity-dependent competitive selection, where replicators compete for scarce binding sites on the catalyst. This mechanism enables efficient selection even within a large replicator pool. Our results provide evidence that the specific catalyst-replicator interactions envisioned in Eigen's hypercycle model can be approximated under dissipative conditions in catalyzed primitive replicator systems.