Oxidative acylation using thioacids.
Several important prebiotic reactions, including the coupling of amino acids into polypeptides by the formation of amide linkages, involve acylation. Theae reactions present a challenge to the understanding of prebiotic synthesis. Condensation reactions relying on dehydrating agents are either inefficient in aqueous solution or require strongly acidic conditions and high temperatures. Activated amino acids such as thioester derivatives have therefore been suggested as likely substrates for prebiotic peptide synthesis. Here we propose a closely related route to amide bond formation involving oxidative acylation by thioacids. We find that phenylalanine, leucine and phenylphosphate are acylated efficiently in aqueous solution by thioacetic acid and an oxidizing agent. From a prebiotic point of view, oxidative acylation has the advantage of proceeding efficiently in solution and under mild conditions. We anticipate that oxidative acylation should prove to be a general method for activating carboxylic acids, including amino acids.
Liu
R
R
The Salk Institute for Biological Studies, San Diego, California 92186, USA.
Orgel
L E
LE
D000215:Acylation; D002851:Chromatography, High Pressure Liquid; D005292:Ferricyanides / Q000737:chemistry; D009570:Nitriles / Q000737:chemistry; D010755:Organophosphates / Q000737:chemistry; D010084:Oxidation-Reduction; D010649:Phenylalanine / Q000737:chemistry; D013438:Sulfhydryl Compounds / Q000737:chemistry*
D005292:Ferricyanides; D009570:Nitriles; D010755:Organophosphates; D013438:Sulfhydryl Compounds; C007931:hexacyanoferrate III; D010649:Phenylalanine; C074782:phenylphosphate; C005732:thioacetic acid