Abstract
We examine the specificity of translation for various primary and secondary amino acid analogues. A synthetase-free, pure, E. coli translation system is used to prevent competing reactions, and three different tRNA adaptor:codon pairs are used to control for tRNA- and codon-specific effects. Surprisingly, N-butyl amino acids fail to incorporate, N-methyl amino acid incorporation efficiencies are dependent on the tRNA adaptor, yet hydroxyPro, Pro, Phe, and Ala incorporate near quantitatively from all adaptors. This suggests that Pro is a privileged N-alkyl amino acid for incorporation by the translation apparatus and establishes that very efficient N-methyl amino acid incorporation is possible if matched with an optimal tRNA adaptor. Results support exploration of Pro analogues and N-methyl amino acids as substrates for engineering ribosomal synthesis of genetically selectable libraries of protease-resistant, N-alkyl peptide ligands.
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