Clindamycin Hydrochloride

Clindamycin hydrochloride binds to the 50S ribosomal subunit and blocks the nascent peptide exit tunnel, thereby inhibiting bacterial protein synthesis. The mechanism of action was investigated using a cell-free system with defined mRNA encoding a short peptide. Clindamycin caused dissociation of peptidyl-tRNA containing two, three or four amino acid residues from the ribosome. This dissociation effect is dependent on the length of the nascent peptide chain. Antibiotics that extend into the peptidyl transferase center, including clindamycin, induce dissociation of short peptidyl-tRNAs, while macrolides such as erythromycin that bind further away from the catalytic center cause dissociation of longer peptidyl-tRNAs containing six to eight residues. These findings demonstrate that clindamycin physically obstructs the passage of the growing peptide chain, leading to premature termination of protein synthesis.

Fig. 1 Clindamycin causes dissociation of di- and tetrapeptidyl-tRNAs from the ribosome during translation. (Tenson T.; et al. 2003)

Clindamycin hydrochloride encapsulated PLA and PLGA nanoparticles were prepared by solvent evaporation method with a drug-to-polymer ratio of 1:10. The optimized nanoparticles exhibited uniform size distribution and monodisperse morphology as confirmed by scanning electron microscopy. DSC and FTIR studies confirmed molecular dispersion of the drug within the polymer matrix without structural alteration. The nanoparticle formulations demonstrated a sustained release profile extending up to 144 hours with controlled release kinetics. Clindamycin-loaded PLA nanoparticles showed enhanced antimicrobial activity against Streptococcus faecalis and Bacillus cereus compared to free drug.

Fig. 2 Demographic and clinical parameters of the patients included in the case-match analysis. (Rauta P R.; et al. 2016)