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Inhibition of bacterial translation and growth by peptide nucleic acids targeted to domain II of 23S rRNA
Author(s) -
XueWen Huang,
Jie Pan,
XianYuan An,
HongXiang Zhuge
Publication year - 2007
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.835
Subject(s) - 23s ribosomal rna , peptide nucleic acid , peptide , tetracycline , translation (biology) , nucleic acid , chemistry , in vitro , ribosomal rna , in vivo , escherichia coli , biochemistry , microbiology and biotechnology , rna , biology , antibiotics , messenger rna , ribosome , gene
The objective of this work was to study the inhibitory effects of antisense peptide nucleic acids (PNAs) targeted to domain II of 23S rRNA on bacterial translation and growth. In this paper, we report that PNA(G1138) or peptide‐PNA(G1138) targeted to domain II of 23S rRNA can inhibit both translation in vitro (in a cell‐free translation system) and bacterial growth in vivo . The inhibitory concentration (IC 50 ) and the minimum inhibiting concentration (MIC) are 0.15 and 10 µ M , respectively. The inhibition effect of PNA(G1138) in vitro is somewhat lower than that of tetracycline (IC 50 = 0.12 µ M ), but the MIC of peptide‐PNA(G1138) against Escherichia coli is significantly higher than that of tetracycline (MIC = 4 µ M ). Further studies based on similar colony‐forming unit (CFU) assays showed that peptide‐PNA(G1138) at 10 µ M is bactericidal, but the bactericidal effect is less effective than that of tetracycline. Nevertheless, the results demonstrated that the peptide‐PNA(G1138) treatment is bactericidal in a dose‐ and sequence‐dependent manner and that the G1138 site of 23S rRNA is a possible sequence target for designing novel PNA‐based antibiotics. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.