A prebiotic template-directed peptide synthesis based on amyloids

Saroj K. Rout, Michael P. Friedmann, Roland Riek () and Jason Greenwald ()
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Saroj K. Rout: Laboratory of Physical Chemistry, ETH Zürich
Michael P. Friedmann: Laboratory of Physical Chemistry, ETH Zürich
Roland Riek: Laboratory of Physical Chemistry, ETH Zürich
Jason Greenwald: Laboratory of Physical Chemistry, ETH Zürich

Nature Communications, 2018, vol. 9, issue 1, 1-8

Abstract: 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-NH2 in the presence of the complementary template peptide Ac-FEFEFEFE-NH2 yields the isotactic product FRFRFRFR-NH2, 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-NH2 and Ac-VDVDVDVDV-NH2 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.

Date: 2018
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DOI: 10.1038/s41467-017-02742-3

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