Adaptability of nonnatural aromatic amino acids to the active center of the E. coli ribosomal A site

Abstract

3'‐N‐Aminoacyl analogs of puromycin with nonnatural aromatic amino acids were synthesized and their inhibitory activity in E.coli in vitro protein synthesizing system was evaluated. The analogs with l‐2‐naphthylalanine, l‐p‐biphenylalanine, l‐2‐anthrylalanine and trans‐l‐p‐phenylazophenylalanine were found to inhibit the protein synthesis with high efficiency. The inhibition suggests that these nonnatural amino acids are accepted by the active center of the E. coli ribosomal A site. A model for the adaptability of nonnatural aromatic amino acids to the active center is proposed.