Agent-based simulations are set to describe the early biotic selection of oligomers made of monomers of different chirality. The simulations consider the spatial distribution of agents and resources, the balance of biomass of different chirality, and the balance of chemical energy. Following the well-known Wald's hypothesis, a disadvantage is attributed to the change in chirality along the biochemical sequence. A racemic amino acid budget is considered, based on findings in meteorites and the results of Miller's experiments. It is also hypothesized that the very first life forms were heterotrophic. Given these assumptions, our simulations showed that biological sequences were not strictly homochiral and had few chirality changes. These results suggest that the current dominance of homochiral species may have been preceded by a more structurally varied biochemistry. This might be reflected in the few known heterochiral proteins, whose structures are based neither on alpha-helices nor on beta-sheets. Extraterrestrial life forms might be based on such heterochiral proteins.
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Article Synopsis
- Researchers designed new D-proteins (50-65 residues) that specifically bind to natural L-proteins, which could be useful in biotechnology.
- These D-proteins showed strong binding affinity to both an artificial L-peptide and important human proteins like TrkA and IL-6, while also effectively inhibiting their signaling in cell studies.
- The study revealed a high-resolution crystal structure of the D-protein-L-peptide complex, confirming the accuracy of the design method and providing insights into the unique interactions between D-proteins and L-peptides.
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