Amino acid esters of 9-(2?,3?-dihydroxypropyl-1?)-adenine are the specific inhibitors of protein synthesis on ribosomes

Abstract
Peptide acceptor properties of phenylalanine and glycine esters of 9′-(2′,3′-dihydroxypropyl-1′)-adenine and 1-(2′,3′-dihydroxypropyl-1′)-4-thiouracyl were investigated. All these esters appeared to be powerful inhibitors of polyphenylalanine synthesis in E. coli MRE-600 ribosomes charged with poly U. Like puromycin, esters of adenine derivatives accepted the AcPhe residue from Ac-[14C] Phe-tRNA in a ribosomal system charged with poly U. However, peptidyl esters of 9-(2′,3′-dihydroxypropyl-1′)-adenine remained bound with ribosomes. The structure of the peptide esters synthesized was ascertained after dissociation of ribosomes into subparticles by direct comparison with the synthetic specimens.