Oligomerization of thioglutamic acid: encapsulated reactions and lipid catalysis

For cellular life to begin on the early Earth, a permeation mechanism would be required to allow polar solutes to enter a membrane-bounded compartment. A second process--internal polymerization of peptides from amino acid--would also be an essential step toward the first compartmented metabolic pathways leading to biosynthesis. Here we report a study of amino acid permeation into lipid vesicles, in which thioglutamic acid penetrated lipid bilayer membranes at rates sufficient to support internal polymerization reactions. We also investigated spontaneous non-enzymatic polymerization reactions of thioglutamic acid to form oligopeptides. We found that oligomers up to 11mers are produced in the reaction mixture, and conclude that certain lipid surfaces can act as catalysts in promoting an oligomerization reaction. These observations are pertinent to understanding processes by which peptide bond synthesis could take place in primitive cellular life on the early Earth.