Clindamycin drug interactions

Albert KS, DeSante KA, Welch RD, DiSanto AR. Pharmacokinetic evaluation of a drug interaction between kaolin-pectin and clindamycin. J Pharm Sci 1978 67 1579-1582. 

Drug Interactions - Absorption half-life of the antibiotic, clindamycin, was prolonged in human subjects when a kaolin-pectin antidiarrheal suspension was coadministered, although the extent of absorption remained the same. On the other hand, both the rate and the extent of absorption of digoxin were lower when it was coadministered with the same kaolin-pectin suspension. Physical absorption and alterations in gut transit time appeared to partly explain the findings. 

Melanin has been shown to form adducts with chloroquine, paraquat, and clindamycin. The significance of drug interaction with melanin has been discussed. 

Drug/Food interactions Food impairs the absorption of lincomycin do not take anything by mouth (except water) for 1 to 2 hours before and after lincomycin. Clindamycin absorption is not affected by food. 

Oral drugs with a markedly bitter taste may lead to poor patient compliance if administered as a solution or syrup. The prodrug approach has been used to improve the taste of chloramphenicol (20), clindamycin, erythromycin, and metronidazole.19 A prodrug such as chloramphenicol palmitate (21), with LogP of around 10, does not dissolve in an appreciable amount in the mouth and, therefore, does not interact with the taste receptors. 

MECHANISM OF ACTION Chloramphenicol inhibits protein synthesis in bacteria, and to a lesser extent, in eukaryotic cells. It binds reversibly to the SOS ribosomal subunit (near the binding site for the macrolide antibiotics and clindamycin). The drug prevents the binding of the amino acid-containing end of the aminoacyl tRNA to the acceptor site on the SOS ribosomal subunit. The interaction between peptidyltransferase and its amino acid substrate is blocked, inhibiting peptide bond formation (Figure 46-2). 

MECHANISM OF ACTION CUndamycin binds to the 50S subunit of bacterial ribosomes and suppresses protein synthesis. Although clindamycin, erythromycin, and chloramphenicol are not structurally related, they act at sites in close proximity (Figures 46-2 and 46-3), and ribosome binding by one of these drugs may inhibit the interaction of the others. MacroUde resistance due to ribosomal methylation also may produce resistance to clindamycin. Because clindamycin does not induce the methylase, there is cross-resistance only if the enzyme is produced constitutively. Clindamycin is not a substrate for macrolide efflux pumps thus, strains that are resistant to macroUdes by this mechanism are susceptible to clindamycin. 

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