Inhibition of Mammalian Mitochondrial Protein Synthesis …

Cell membrane inhibitors disorganize the structure or inhibit the function of bacterial membranes. The integrity of the cytoplasmic and outer membranes is vital to bacteria, and compounds that disorganize the membranes rapidly kill the cells. However, due to the similarities in phospholipids in eubacterial and eukaryotic membranes, this action is rarely specific enough to permit these compounds to be used systemically. The only antibacterial antibiotic of clinical importance that acts by this mechanism is Polymyxin, produced by Bacillus polymyxis. Polymyxin is effective mainly against Gram-negative bacteria and is usually limited to topical usage. Polymyxins bind to membrane phospholipids and thereby interfere with membrane function. Polymyxin is occasionally given for urinary tract infections caused by Pseudomonas that are gentamicin, carbenicillin and tobramycin resistant. The balance between effectiveness and damage to the kidney and other organs is dangerously close, and the drug should only be given under close supervision in the hospital.

Effect of chloramphenicol on protein synthesis in e

The inhibitory effect of chloramphenicol on the synthesis of antibody in tissue culture (1963)

Inhibition of Protein Synthesis by Chloramphenicol, …

Soon after Gale & Folkes ( 1) first reported this inhibitory effect in bacteria, it became apparent that mammalian cells were remarkable resistant to chloramphenicol and that no discernible effects were demonstrable in mammalian systems unless excessive amounts of the drug were employed.

To elucidate the role of protein synthesis in DNA formation, E

It has been suggested that the inability of chloramphenicol in pharmacologic concentrations to inhibit mammalian protein synthesis accounts for the selectivity of the antibiotic for bacteria.

Inhibition of polyuridylic acid‐induced ribosomal protein synthesis by chloramphenicol
Effects of chloramphenicol upon a ribosomal amino acid polymerization system and its binding to bacterial ribosome


Chloramphenicol has a broad spectrum of activity but it exerts a bacteriostatic effect. It is effective against intracellular parasites such as the rickettsiae. Unfortunately, aplastic anemia, which is dose related develops in a small proportion (1/50,000) of patients. Chloramphenicol was originally discovered and purified from the fermentation of a , but currently it is produced entirely by chemical synthesis. Chloramphenicol inhibits the bacterial enzyme peptidyl transferase thereby preventing the growth of the polypeptide chain during protein synthesis.

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The effect of chloramphenicol on synthesis of …

Eukaryotic cells are generally not affected by chloramphenicol. Nevertheless, the clinical application of this drug for the treatment of systemic infections has been severely curtailed, primarily because of the haematotoxicity associated with its use. Chloramphenicol continues to be used topically, particularly in the treatment of eye infections. The emergence of chloramphenicol-resistant bacteria, apparently in response to the selective pressure exerted by the drug (see Antibiotic Resistance), has also restricted the use of chloramphenicol in the treatment of bacterial infections.

Effect of some antibiotics on the protein synthesis in cell suspensions and on the peptidyl transferase in cell‐free systems

4 Important Inhibitors of Protein Synthesis

Chloramphenicol resistance by enzymatic modification in both Gram-positive and Gram-negative bacteria can be either constitutive or inducible. What is unusual about inducible chloramphenicol resistance is that it occurs by translational attenuation, rather than by transcriptional attenuation. The ribosome-binding site for the resistance determinant is sequestered in a secondary "hairpin" structure situated within the encoding mRNA; a short, translated open reading frame, termed the leader, lies upstream of this structure. In the absence of the antibiotic, the secondary structure is maintained, the ribosome does not translate the mRNA that constitutes the hairpin, and the resistance gene is not translated. In the presence of the antibiotic, the ribosome stalls at the leader sequence and the secondary structure relaxes, allowing the cat (or cml) determinant to be translated (18) (Fig. 6).