'Reverse chemical evolution': A new method to search for thermally stable biopolymers

Abstract

The primitive sea on Earth may have had high-temperature and high-pressure conditions similar to those in present-day hydrothermal environments. If life originated in the hot sea, thermal stability of the constituent molecules would have been necessary. Thus far, however, it has been reported that biopolymers hydrolyze too rapidly to support life at temperatures of more than 200°C. We herein propose a novel approach, called reverse chemical evolution, to search for biopolymers notably more stable against thermal decomposition than previously reported. The essence of the approach is that hydrolysis of a protein or functional RNA (m-, t-, r-RNA) at high temperature and high pressure simulating the ancient sea environment may yield thermally stable peptides or RNAs at higher concentrations than other peptides or RNAs. An experimental test hydrolyzing bovine ribonuclease A in aqueous solution at 205°C and 25 MPa yielded three prominently stable molecules weighing 859, 1030 and 695 Da. They are thermally some tens or hundreds times more stable than a polyglycine of comparable mass. Sequence analyses of the 859- and 1030-Da molecules revealed that they are a heptapeptide and its homologue, respectively, elongated by two amino acids at the N-terminal region, originally embedded as residues 112-120 in the protein. They consist mainly of hydrophobic amino acids.