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Nucleic Acids Research, 1974, Vol. 1, No. 10 1221-1332
© 1974

Articles

The inhibition of peptidyl transferase activity by aminoacyl derivatives of some nucleoside aliphatic analogues

A. Holy, J. Cerná and I. Rychllk

Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences 166 10 Prague 6, Flemingovo 2, Czechoslovakia

Received July 12, 1974. Aminoacyl (Phe, Gly) derivatives of nucleoside aliphatic analogues bearing a hydroxyalkyl chain have been prepared by the condensation of the alcohols with N-benzyloxycarbonylamino acid in the presence of DCC followed by hydrogenolysis in methanol. These compounds inhibit peptidyl transferase activity and binding of acceptor substrate to E. coli ribosomes. The inhibitory activity is not much affected by the nature of either the aminoacyl or the heterocyclic base residue. In the transfer reaction, no peptide bond formation occurs with the above compounds as acceptors.


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