Formation of peptide bonds from metastable versus crystalline phase: implications for the origin of life.
Formation of peptide bonds was attempted by thermal activation of dry amino acids from aqueous solution that simulated prebiotic evaporative environments. The evaporation trend of amino acids solutions shows a bifurcation and can lead to either a crystalline phase (near equilibrium) or a metastable non-crystalline phase (far from equilibrium). Only amino acids in this metastable phase are able to form peptide bonds by thermal activation at temperatures that are generated by solar radiation today. We suggest that this metastable phase is the ideal initial material to trigger amino acid assemblage with protein-like structure because provide the driving force (supersaturation) for an intense interaction between monomers of different amino acids and allows activation of these monomers in plausible prebiotic conditions.
Viedma
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Departamento Cristalografia-Mineralogia, Universidad Complutense, Facultad Geologia, 28040, Madrid, Spain. Viedma@eucmax.sim.ucm.es
D000596:Amino Acids / Q000737:chemistry*; D005075:Biological Evolution; D003460:Crystallization; D019418:Evolution, Chemical; D000069497:Origin of Life; D010455:Peptides / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D000596:Amino Acids; D010455:Peptides; D011506:Proteins