Abstract
The most common theory about the emergence of prebiotic amino acids can’t account for cysteine, so origin-of-life researchers have proposed that it is a product of evolution. A new study proposes a prebiotic route for making cysteine-containing compounds. In addition, Matthew W. Powner and coworkers at University College London show a plausible prebiotic pathway in which these compounds catalyze the synthesis of peptides containing other amino acids ( Science 2020, DOI: 10.1126/science.abd5680 ). They propose a prebiotic pathway that starts with serine nitrile. First, a reaction with thioacetic acid forms diacetylated serine nitrile. Over 4 days, it converts to acetylated dehydroalanine nitrile. Finally, reaction with hydrogen sulfide results in acetylcysteine-containing compounds. The researchers then show that those compounds can catalyze peptide ligation. In water at neutral pH, the acylcysteines catalyzed the reaction of acylglycine nitrile with all canonical amino acids to form simple peptides. “The inherent catalytic activity of simple
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