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.
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