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Mechanism of Action of Erythromycin, Azithromycin, Clarithromycin, Chloramphenicol, and Clindamycin

Dr. Najeeb Lectures via YouTube

Overview

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This lecture explains how clindamycin, macrolides, and chloramphenicol inhibit bacterial protein synthesis, focusing on their actions at the 50S ribosomal subunit and their effects on peptide chain elongation.

Syllabus

Introduction and overview of lecture
Overview of similarities between Clindamycin, Macrolide and chloramphenicol
Clindamycin, macrolide Erythromycin and chloramphenicol work as protein synthesis inhibitors
MOA of clindamycin, macrolide Erythromycin and chloramphenicol on Bacterial Ribosomes
MOA of clindamycin, macrolide Erythromycin and chloramphenicol on larger 50s ribosomal subunit
Action of clindamycin , macrolide Erythromycin and Chloramphenicol on 23s Ribosomal RNA
Summary of above 4 similarities in the MOA of Clindamycin , Macrolide Erythromycin and Chloramphenicol
MOA of Clindamycin, Macrolide Erythromycin and Chloramphenicol on Ribozyme
What is Peptidyl Transferase?
Summary of all above similarities between Clindamycin, Macrolide Erythromycin and Chloramphenicol
Detailed explanation on the functions of Peptidyl Transferase
Transpeptidation and Ribosomal Translocation
Peptide chain elongation
How Clindamycin, Macrolide Erythromycin and chloramphenicol inhibit the protein synthesis by inhibiting the chain elongation process?
Summary of similarities between Clindamycin, Macrolide Erythromycin and Chloramphenicol
MOA; Clindamycin
MOA; Clindamycin as bacteriostatic and bactericidal
Summary of MOA of Clindamycin
MOA; Macrolides Erythromycin
MOA; Chloramphenicol binding site.
MOA; Comparison of binding site of clindamycin vs macrolide vs chloramphenicol.
MOA; Chloramphenicol.

Taught by

Dr. Najeeb Lectures

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