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Updated: Feb 3, 2026

Light-driven Enzymatic Decarboxylation

Light-driven Enzymatic Decarboxylation

Published on: May 22, 2016

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

Éva Bartus¹, Edit Wéber^1,2, Attila Tököli^1,3

¹Department of Medical Chemistry, University of Szeged, Szeged, Hungary.

Angewandte Chemie (International Ed. in English)

|February 2, 2026

Summary

A flexible protein, calmodulin, was shown to catalyze primitive peptide replication using UVA light. This process enables competitive selection, mimicking early life evolution under resource limitations.

Keywords:

catalyzed replication competitive selection dissipative foldamer light‐driven disulfide rearrangement

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Area of Science:

Biochemistry
Origin of Life Research
Systems Chemistry

Background:

Theoretical models suggest catalytic molecules are crucial for the emergence of life.
Autocatalytic replication cycles are a key component in prebiotic evolution theories.
Protein catalysts could potentially facilitate the formation and replication of primitive biomolecules.

Purpose of the Study:

To investigate if a protein catalyst can create conditions for proximity-controlled, dissipative replication of primitive peptides.
To explore the role of a limited resource catalyst in competitive selection during prebiotic replication.
To demonstrate a mechanism for efficient selection within a large pool of replicators.

Main Methods:

Utilized a helical foldamer-based replicator system.
Employed calmodulin, a structurally flexible and promiscuous protein, as the catalyst.
Applied UVA light to drive the replication process.
Analyzed the system's response to varying light intensities and catalyst availability.

Main Results:

Calmodulin was shown to catalyze UVA light-driven replication of the foldamer system.
The protein accelerated both non-autocatalytic synthesis and autocatalytic replication, with the latter being dominant.
The system exhibited light-intensity-dependent competitive selection, where replicators competed for catalyst binding sites.
Efficient selection was observed even within a large replicator pool.

Conclusions:

Protein catalysts, like calmodulin, can facilitate dissipative, proximity-controlled replication of primitive peptides.
Competitive selection for limited catalyst resources is a viable mechanism for early life evolution.
The findings support theoretical models, such as Eigen's hypercycle, under dissipative conditions in catalyzed primitive replicator systems.