A prebiotic template-directed peptide synthesis based on amyloids.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 29339755.
- Also identified by DOI 10.1038/s41467-017-02742-3 and PMC identifier 5770463.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
The prebiotic replication of information-coding molecules is a central problem concerning life's origins. Here, we report that amyloids composed of short peptides can direct the sequence-selective, regioselective and stereoselective condensation of amino acids. The addition of activated DL-arginine and DL-phenylalanine to the peptide RFRFR-NH<sub>2</sub> in the presence of the complementary template peptide Ac-FEFEFEFE-NH<sub>2</sub> yields the isotactic product FRFRFRFR-NH<sub>2</sub>, 1 of 64 possible triple addition products, under conditions in which the absence of template yields only single and double additions of mixed stereochemistry. The templating mechanism appears to be general in that a different amyloid formed by (Orn)V(Orn)V(Orn)V(Orn)V-NH<sub>2</sub> and Ac-VDVDVDVDV-NH<sub>2</sub> is regioselective and stereoselective for N-terminal, L-amino-acid addition while the ornithine-valine peptide alone yields predominantly sidechain condensation products with little stereoselectivity. Furthermore, the templating reaction is stable over a wide range of pH (5.6-8.6), salt concentration (0-4 M NaCl), and temperature (25-90 °C), making the amyloid an attractive model for a prebiotic peptide replicating system.
Medical subject headings
- Amino Acids
- Amyloid
- Chemistry Techniques, Synthetic
- Peptides