Complementary carrier peptide synthesis: General strategy and implications for prebiotic origin of peptide synthesis (oligonucleotides/templates/catalysis/peptidyl esters)

A method for peptide synthesis is Proposed based on a template-directed scheme that parallels thiat of the native ribosomal mechanism. In this procedure, peptide bond formation is facilitated by the juxtaposition of aminoacyl and peptidyl oligonucleotide carriers bound adjacent to one another on an oligonucleotide template. The general strategy of the synthesis and relevant model studies are described. The scheme provides an intrinsic mechanism by which oligonucleotides can direct the synthesis of polypeptides in the absence of protein or ribosomal machinery and, as such, suggests a model for the origin of prebiotic protein synthesis. With current chemical methods of peptide synthesis, fidelity of the coupling reaction is achieved by the use of a temporary protecting group on either the amine or carboxyl function of the incoming amino acid. For example, for a synthesis from the NH2 terminus, an ester might serve in this role: